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Literature summary for 7.2.2.14 extracted from

  • Maguire, M.E.
    Magnesium transporters: properties, regulation and structure (2006), Front. Biosci., 11, 3149-3163.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene corA, DNA and amino acid asequence determination Escherichia coli
gene corA, DNA and amino acid asequence determination Arabidopsis thaliana
gene corA, DNA and amino acid asequence determination Thermotoga maritima
gene corA, DNA and amino acid sequence determination Methanocaldococcus jannaschii
gene mgtE, expression in and functional complementation of a CorA Mg2+ transport mutant of Salmonella enterica serovar Thyphimurium Cytobacillus firmus
gene mgtE, expression in and functional complementation of a CorA Mg2+ transport mutant of Salmonella enterica serovar Thyphimurium Providencia stuartii
genes mgtA and mgtB, from complementation of the Mg2+ growth phenotype mutants MM7 and MM281, gene corA, DNA and amino acid sequence determination, the corA promoter does not respond to extracellular Mg2+ concentration, transcription factor PhoP is important in corA transcription regulation, overview Salmonella enterica subsp. enterica serovar Typhimurium

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure analysis from PDB ID BBJ2 at 3.9 A resolution for the whole enzyme, and at 1.8 A resolution for the soluble domain, overview Thermotoga maritima

Protein Variants

Protein Variants Comment Organism
additional information mutant atmrs2-2 lacks any domain sufficiently hydrophobic to insert in a membrane and does not complement the yeast mutant, as does sibling atmrs2-1 Arabidopsis thaliana
additional information mutations of mgtA, mgtB, and corA result in protein incapable of Mg2+ ransport, the Mg2+ transport mutant MM281 can be rescued by complementation with corA from Bacillus firmus strain OB4 or Providencia stuartii, mutation of corA leads to attenuation of virulence and to other defects, but not to growth defects, the CorA-mediated Ni2+ uptake is 2fold increased in a phoP strain compared to wild-type without any increase in the amount of CorA protein Salmonella enterica subsp. enterica serovar Typhimurium

Inhibitors

Inhibitors Comment Organism Structure
Ca2+ inhibition of MgtE Cytobacillus firmus
Ca2+ weak inhibition of CorA, MgtA, and MgtB Salmonella enterica subsp. enterica serovar Typhimurium
Co2+ inhibition of MgtA and MgtB Salmonella enterica subsp. enterica serovar Typhimurium
Mn2+ inhibition of MgtE Cytobacillus firmus
Mn2+ weak, noncompetitive inhibition Escherichia coli
Mn2+ inhibition of CorA, MgtA, and MgtB, inhibition of CorA is noncompetitive, maximal 35% inhibition of MgtA at over 1 mM Salmonella enterica subsp. enterica serovar Typhimurium
additional information no inhibition of MgtE by Ba2+ Cytobacillus firmus
additional information no inhibition of CorA by Fe2+ and Fe3+ Salmonella enterica subsp. enterica serovar Typhimurium
Ni2+ slight inhibition of MgtE Cytobacillus firmus
Sr2+ inhibition of MgtE Cytobacillus firmus
Zn2+ inhibition of MgtE Cytobacillus firmus
Zn2+ inhibition of MgtA Salmonella enterica subsp. enterica serovar Typhimurium

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Mg2+ uptake kinetics for CorA Salmonella enterica subsp. enterica serovar Typhimurium
0.002
-
Ni2+ pH 7.4, 37°C, MgtB Salmonella enterica subsp. enterica serovar Typhimurium
0.005
-
Ni2+ pH 7.4, 37°C, MgtA Salmonella enterica subsp. enterica serovar Typhimurium
0.006
-
Mg2+ pH 7.4, 37°C, MgtB Salmonella enterica subsp. enterica serovar Typhimurium
0.01 0.015 Mg2+ pH 7.4, 37°C, CorA Salmonella enterica subsp. enterica serovar Typhimurium
0.02 0.03 Co2+ pH 7.4, 37°C, CorA Salmonella enterica subsp. enterica serovar Typhimurium
0.03
-
Mg2+ pH 7.4, 37°C, MgtA Salmonella enterica subsp. enterica serovar Typhimurium
0.04
-
Co2+ pH 7.4, 37°C, CorA Escherichia coli
0.05
-
Mg2+ pH 7.4, 37°C, MgtE Cytobacillus firmus
0.08
-
Co2+ pH 7.4, 37°C, MgtE Cytobacillus firmus
0.2
-
Ni2+ pH 7.4, 37°C, CorA Salmonella enterica subsp. enterica serovar Typhimurium
0.4
-
Ni2+ pH 7.4, 37°C, CorA Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Salmonella enterica subsp. enterica serovar Typhimurium 16020
-
membrane
-
Escherichia coli 16020
-
membrane
-
Arabidopsis thaliana 16020
-
membrane
-
Mycobacterium tuberculosis 16020
-
membrane
-
Aeromonas hydrophila 16020
-
membrane
-
Cytobacillus firmus 16020
-
membrane
-
Providencia stuartii 16020
-
membrane
-
Methanosarcina sp. 16020
-
membrane
-
Thermotoga maritima 16020
-
membrane
-
Methanothermobacter sp. 16020
-
membrane
-
Methanocaldococcus jannaschii 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
additional information no or poor inhibition of CorA by Ca2+, Sr2+, Ba2+, Zn2+, Fe2+, and Fe3+ Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
42000
-
5 * 42000, about, SDS-PAGE Escherichia coli
42000
-
5 * 42000, about, SDS-PAGE Arabidopsis thaliana
42000
-
5 * 42000, about, SDS-PAGE Methanocaldococcus jannaschii
42000
-
5 * 42000, about, SDS-PAGE, a funnel-shaped homopentamer with two transmembrane helices per monomer, the large cytosolic domain forms the funnel, overview Thermotoga maritima
42000
-
5 * 42000, about, SDS-PAGE, CorA is a homopentamer with two transmembrane domains per monomer, the first of which forms the ion conduction pathway, CorA structure analysis, overview Salmonella enterica subsp. enterica serovar Typhimurium

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + Mg2+/out Escherichia coli
-
ADP + phosphate + Mg2+/in
-
?
ATP + H2O + Mg2+/out Arabidopsis thaliana
-
ADP + phosphate + Mg2+/in
-
?
ATP + H2O + Mg2+/out Mycobacterium tuberculosis
-
ADP + phosphate + Mg2+/in
-
?
ATP + H2O + Mg2+/out Aeromonas hydrophila
-
ADP + phosphate + Mg2+/in
-
?
ATP + H2O + Mg2+/out Cytobacillus firmus
-
ADP + phosphate + Mg2+/in
-
?
ATP + H2O + Mg2+/out Providencia stuartii
-
ADP + phosphate + Mg2+/in
-
?
ATP + H2O + Mg2+/out Methanosarcina sp.
-
ADP + phosphate + Mg2+/in
-
?
ATP + H2O + Mg2+/out Thermotoga maritima
-
ADP + phosphate + Mg2+/in
-
?
ATP + H2O + Mg2+/out Methanothermobacter sp.
-
ADP + phosphate + Mg2+/in
-
?
ATP + H2O + Mg2+/out Methanocaldococcus jannaschii
-
ADP + phosphate + Mg2+/in
-
?
ATP + H2O + Mg2+/out Salmonella enterica subsp. enterica serovar Typhimurium CorA and MgtE are not transcriptionally regulated ADP + phosphate + Mg2+/in
-
?
ATP + H2O + Mg2+/out Cytobacillus firmus OF4
-
ADP + phosphate + Mg2+/in
-
?

Organism

Organism UniProt Comment Textmining
Aeromonas hydrophila
-
gene mgtE
-
Arabidopsis thaliana
-
gene corA
-
Cytobacillus firmus
-
-
-
Cytobacillus firmus OF4
-
-
-
Escherichia coli
-
gene corA
-
Methanocaldococcus jannaschii Q58439 gene corA
-
Methanosarcina sp.
-
gene mgtC
-
Methanothermobacter sp.
-
gene mgtC
-
Mycobacterium tuberculosis
-
gene mgtC
-
Providencia stuartii
-
gene mgtE
-
Salmonella enterica subsp. enterica serovar Typhimurium
-
genes corA, mgtA/B, mgtE
-
Thermotoga maritima Q9WZ31 gene corA
-

Reaction

Reaction Comment Organism Reaction ID
ATP + H2O + Mg2+[side 1] = ADP + phosphate + Mg2+[side 2] Mg2+ transport involves first the binding of the fully hydrated ion to an extracellular binding loop connecting the transmembrane domain, passage through the membrane, not involving electrostatic interactions but two cytsolic domains, one with extremely high positive charges and the other with negative charge helping to control the Mg2+ flux in concert with an intracellular Mg2+ bound between the domains of each monomer, transport mechanism, overview Salmonella enterica subsp. enterica serovar Typhimurium
ATP + H2O + Mg2+[side 1] = ADP + phosphate + Mg2+[side 2] Mg2+ transport involves first the binding of the fully hydrated ion to an extracellular binding loop connecting the transmembrane domain, passage through the membrane, not involving electrostatic interactions but two cytsolic domains, one with extremely high positive charges and the other with negative charge helping to control the Mg2+ flux in concert with an intracellular Mg2+ bound between the domains of each monomer, transport mechanism, overview Escherichia coli
ATP + H2O + Mg2+[side 1] = ADP + phosphate + Mg2+[side 2] Mg2+ transport involves first the binding of the fully hydrated ion to an extracellular binding loop connecting the transmembrane domain, passage through the membrane, not involving electrostatic interactions but two cytsolic domains, one with extremely high positive charges and the other with negative charge helping to control the Mg2+ flux in concert with an intracellular Mg2+ bound between the domains of each monomer, transport mechanism, overview Arabidopsis thaliana
ATP + H2O + Mg2+[side 1] = ADP + phosphate + Mg2+[side 2] Mg2+ transport involves first the binding of the fully hydrated ion to an extracellular binding loop connecting the transmembrane domain, passage through the membrane, not involving electrostatic interactions but two cytsolic domains, one with extremely high positive charges and the other with negative charge helping to control the Mg2+ flux in concert with an intracellular Mg2+ bound between the domains of each monomer, transport mechanism, overview Mycobacterium tuberculosis
ATP + H2O + Mg2+[side 1] = ADP + phosphate + Mg2+[side 2] Mg2+ transport involves first the binding of the fully hydrated ion to an extracellular binding loop connecting the transmembrane domain, passage through the membrane, not involving electrostatic interactions but two cytsolic domains, one with extremely high positive charges and the other with negative charge helping to control the Mg2+ flux in concert with an intracellular Mg2+ bound between the domains of each monomer, transport mechanism, overview Aeromonas hydrophila
ATP + H2O + Mg2+[side 1] = ADP + phosphate + Mg2+[side 2] Mg2+ transport involves first the binding of the fully hydrated ion to an extracellular binding loop connecting the transmembrane domain, passage through the membrane, not involving electrostatic interactions but two cytsolic domains, one with extremely high positive charges and the other with negative charge helping to control the Mg2+ flux in concert with an intracellular Mg2+ bound between the domains of each monomer, transport mechanism, overview Cytobacillus firmus
ATP + H2O + Mg2+[side 1] = ADP + phosphate + Mg2+[side 2] Mg2+ transport involves first the binding of the fully hydrated ion to an extracellular binding loop connecting the transmembrane domain, passage through the membrane, not involving electrostatic interactions but two cytsolic domains, one with extremely high positive charges and the other with negative charge helping to control the Mg2+ flux in concert with an intracellular Mg2+ bound between the domains of each monomer, transport mechanism, overview Providencia stuartii
ATP + H2O + Mg2+[side 1] = ADP + phosphate + Mg2+[side 2] Mg2+ transport involves first the binding of the fully hydrated ion to an extracellular binding loop connecting the transmembrane domain, passage through the membrane, not involving electrostatic interactions but two cytsolic domains, one with extremely high positive charges and the other with negative charge helping to control the Mg2+ flux in concert with an intracellular Mg2+ bound between the domains of each monomer, transport mechanism, overview Methanosarcina sp.
ATP + H2O + Mg2+[side 1] = ADP + phosphate + Mg2+[side 2] Mg2+ transport involves first the binding of the fully hydrated ion to an extracellular binding loop connecting the transmembrane domain, passage through the membrane, not involving electrostatic interactions but two cytsolic domains, one with extremely high positive charges and the other with negative charge helping to control the Mg2+ flux in concert with an intracellular Mg2+ bound between the domains of each monomer, transport mechanism, overview Thermotoga maritima
ATP + H2O + Mg2+[side 1] = ADP + phosphate + Mg2+[side 2] Mg2+ transport involves first the binding of the fully hydrated ion to an extracellular binding loop connecting the transmembrane domain, passage through the membrane, not involving electrostatic interactions but two cytsolic domains, one with extremely high positive charges and the other with negative charge helping to control the Mg2+ flux in concert with an intracellular Mg2+ bound between the domains of each monomer, transport mechanism, overview Methanothermobacter sp.
ATP + H2O + Mg2+[side 1] = ADP + phosphate + Mg2+[side 2] Mg2+ transport involves first the binding of the fully hydrated ion to an extracellular binding loop connecting the transmembrane domain, passage through the membrane, not involving electrostatic interactions but two cytsolic domains, one with extremely high positive charges and the other with negative charge helping to control the Mg2+ flux in concert with an intracellular Mg2+ bound between the domains of each monomer, transport mechanism, overview Methanocaldococcus jannaschii

Source Tissue

Source Tissue Comment Organism Textmining
additional information constitutive expression of corA Salmonella enterica subsp. enterica serovar Typhimurium
-
additional information constitutive expression of MgtE Aeromonas hydrophila
-
additional information constitutive expression of MgtE Cytobacillus firmus
-
additional information constitutive expression of MgtE Providencia stuartii
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + Co2+/out
-
Escherichia coli ADP + phosphate + Co2+/in
-
?
ATP + H2O + Co2+/out
-
Cytobacillus firmus ADP + phosphate + Co2+/in
-
?
ATP + H2O + Co2+/out
-
Methanocaldococcus jannaschii ADP + phosphate + Co2+/in
-
?
ATP + H2O + Co2+/out transported by CorA Salmonella enterica subsp. enterica serovar Typhimurium ADP + phosphate + Co2+/in
-
?
ATP + H2O + Co2+/out
-
Cytobacillus firmus OF4 ADP + phosphate + Co2+/in
-
?
ATP + H2O + Mg2+/out
-
Escherichia coli ADP + phosphate + Mg2+/in
-
?
ATP + H2O + Mg2+/out
-
Arabidopsis thaliana ADP + phosphate + Mg2+/in
-
?
ATP + H2O + Mg2+/out
-
Mycobacterium tuberculosis ADP + phosphate + Mg2+/in
-
?
ATP + H2O + Mg2+/out
-
Aeromonas hydrophila ADP + phosphate + Mg2+/in
-
?
ATP + H2O + Mg2+/out
-
Cytobacillus firmus ADP + phosphate + Mg2+/in
-
?
ATP + H2O + Mg2+/out
-
Providencia stuartii ADP + phosphate + Mg2+/in
-
?
ATP + H2O + Mg2+/out
-
Methanosarcina sp. ADP + phosphate + Mg2+/in
-
?
ATP + H2O + Mg2+/out
-
Thermotoga maritima ADP + phosphate + Mg2+/in
-
?
ATP + H2O + Mg2+/out
-
Methanothermobacter sp. ADP + phosphate + Mg2+/in
-
?
ATP + H2O + Mg2+/out
-
Methanocaldococcus jannaschii ADP + phosphate + Mg2+/in
-
?
ATP + H2O + Mg2+/out CorA and MgtE are not transcriptionally regulated Salmonella enterica subsp. enterica serovar Typhimurium ADP + phosphate + Mg2+/in
-
?
ATP + H2O + Mg2+/out transported by CorA, MgtA, and MgtB Salmonella enterica subsp. enterica serovar Typhimurium ADP + phosphate + Mg2+/in
-
?
ATP + H2O + Mg2+/out
-
Cytobacillus firmus OF4 ADP + phosphate + Mg2+/in
-
?
ATP + H2O + Ni2+/out
-
Escherichia coli ADP + phosphate + Ni2+/in
-
?
ATP + H2O + Ni2+/out
-
Methanocaldococcus jannaschii ADP + phosphate + Ni2+/in
-
?
ATP + H2O + Ni2+/out transported by CorA, MgtA, and MgtB Salmonella enterica subsp. enterica serovar Typhimurium ADP + phosphate + Ni2+/in
-
?
additional information CorA does not contain an ATP binding site and acts as a Mg2+ channel probably driven by the inward electrochemical Mg2+ potential Escherichia coli ?
-
?
additional information CorA does not contain an ATP binding site and acts as a Mg2+ channel probably driven by the inward electrochemical Mg2+ potential Thermotoga maritima ?
-
?
additional information CorA does not contain an ATP binding site and acts as a Mg2+ channel probably driven by the inward electrochemical Mg2+ potential Methanocaldococcus jannaschii ?
-
?
additional information CorA does not contain an ATP binding site and acts as a Mg2+ channel probably driven by the inward electrochemical Mg2+ potential, the different cation influx activities do not influence each other activity, MgtA and MgtB are P-type ATPases Salmonella enterica subsp. enterica serovar Typhimurium ?
-
?
additional information the Arabidopsis thaliana CorA homologues of the Mrs2p family have putative transmembrane segments and catalyzes Mg2+ transport, CorA does not contain an ATP binding site and acts as a Mg2+ channel probably driven by the inward electrochemical Mg2+ potential Arabidopsis thaliana ?
-
?

Subunits

Subunits Comment Organism
More secondary structure determination Thermotoga maritima
pentamer 5 * 42000, about, SDS-PAGE Escherichia coli
pentamer 5 * 42000, about, SDS-PAGE Arabidopsis thaliana
pentamer 5 * 42000, about, SDS-PAGE Methanocaldococcus jannaschii
pentamer 5 * 42000, about, SDS-PAGE, a funnel-shaped homopentamer with two transmembrane helices per monomer, the large cytosolic domain forms the funnel, overview Thermotoga maritima
pentamer 5 * 42000, about, SDS-PAGE, CorA is a homopentamer with two transmembrane domains per monomer, the first of which forms the ion conduction pathway, CorA structure analysis, overview Salmonella enterica subsp. enterica serovar Typhimurium

Synonyms

Synonyms Comment Organism
CorA
-
Salmonella enterica subsp. enterica serovar Typhimurium
CorA
-
Escherichia coli
CorA
-
Thermotoga maritima
CorA
-
Methanocaldococcus jannaschii
CorA/Mrs2p
-
Arabidopsis thaliana
magnesium transporter
-
Salmonella enterica subsp. enterica serovar Typhimurium
Mg2+ transporter
-
Salmonella enterica subsp. enterica serovar Typhimurium
MgtA
-
Salmonella enterica subsp. enterica serovar Typhimurium
MgtB
-
Salmonella enterica subsp. enterica serovar Typhimurium
MgtC
-
Mycobacterium tuberculosis
MgtC
-
Methanosarcina sp.
MgtC
-
Methanothermobacter sp.
MgtE
-
Salmonella enterica subsp. enterica serovar Typhimurium
MgtE
-
Aeromonas hydrophila
MgtE
-
Cytobacillus firmus
MgtE
-
Providencia stuartii
More MgtA/B transporters belong to the P-type ATPase superfamily Salmonella enterica subsp. enterica serovar Typhimurium

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Salmonella enterica subsp. enterica serovar Typhimurium
37
-
assay at Escherichia coli
37
-
assay at Cytobacillus firmus
37
-
assay at Methanocaldococcus jannaschii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
assay at Salmonella enterica subsp. enterica serovar Typhimurium
7.4
-
assay at Cytobacillus firmus
7.4
-
assay at Methanocaldococcus jannaschii

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.007
-
Zn2+ pH 7.4, 37°C, MgtA Salmonella enterica subsp. enterica serovar Typhimurium
0.008
-
Co2+ pH 7.4, 37°C, MgtB Salmonella enterica subsp. enterica serovar Typhimurium
0.02
-
Zn2+ pH 7.4, 37°C, MgtE Cytobacillus firmus
0.03
-
Mn2+ pH 7.4, 37°C, CorA Salmonella enterica subsp. enterica serovar Typhimurium
0.04
-
Co2+ pH 7.4, 37°C, MgtA Salmonella enterica subsp. enterica serovar Typhimurium
0.04
-
Mn2+ pH 7.4, 37°C, MgtB Salmonella enterica subsp. enterica serovar Typhimurium
0.05
-
Ca2+ pH 7.4, 37°C, MgtE Cytobacillus firmus
0.07
-
Mn2+ pH 7.4, 37°C, MgtE Cytobacillus firmus
0.08
-
Sr2+ pH 7.4, 37°C, MgtE Cytobacillus firmus
0.2
-
Ni2+ pH 7.4, 37°C, MgtE, above Cytobacillus firmus
0.3
-
Ca2+ pH 7.4, 37°C, MgtA Salmonella enterica subsp. enterica serovar Typhimurium
5
-
Ca2+ pH 7.4, 37°C, CorA Salmonella enterica subsp. enterica serovar Typhimurium
30
-
Ca2+ pH 7.4, 37°C, MgtB Salmonella enterica subsp. enterica serovar Typhimurium