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Literature summary for 7.3.2.1 extracted from

  • Vyas, N.K.; Vyas, M.N.; Quiocho, F.A.
    Crystal structure of M tuberculosis ABC phosphate transport receptor: specificity and charge compensation dominated by ion-dipole interactions (2003), Structure, 11, 765-774.
    View publication on PubMed
Search for more literature for 7.3.2.1

Crystallization (Commentary)

Crystallization (Comment) Organism
MIR method Mycobacterium tuberculosis

Localization

Localization Comment Organism GeneOntology No. Textmining
cell wall on the surface of the outer Mycobacterium tuberculosis 5618
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
38000
-
 SDS-PAGE Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + phosphate/out Mycobacterium tuberculosis import of phosphate ADP + phosphate + phosphate/in
-
 ?

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
no modification
-
 Mycobacterium tuberculosis

Purification (Commentary)

Purification (Comment) Organism
-
 Mycobacterium tuberculosis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + phosphate/out import of phosphate Mycobacterium tuberculosis ADP + phosphate + phosphate/in
-
 ?

Synonyms

Synonyms Comment Organism
ABC phosphate transport receptor
-
 Mycobacterium tuberculosis
phosphate-bound PstS-1
-
 Mycobacterium tuberculosis
phosphate-specific transport substrate binding protein-1
-
 Mycobacterium tuberculosis
Pst
-
 Mycobacterium tuberculosis