Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.7.7.65 extracted from

  • Xu, M.; Wang, Y.Z.; Yang, X.A.; Jiang, T.; Xie, W.
    Structural studies of the periplasmic portion of the diguanylate cyclase CdgH from Vibrio cholerae (2017), Sci. Rep., 7, 1861 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.7.65

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of the C-terminally His6-tagged CdgH periplasmic portion (residues 46-491) including the tandem PBPb-I and PBPb-II domains of the enzyme Vibrio cholerae serotype O1

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant periplasmic portion (residues 46-491, which includes the tandem PBPb-I and PBPb-II domains) of C-terminally His6-tagged CdgH, X-ray diffraction structure determination and analysis at 2.6 A resolution Vibrio cholerae serotype O1

Protein Variants

Protein Variants Comment Organism
additional information ITC analysis of interactions between different amino acids and the periplasmic portion of CdgH with different truncations and mutants, overview Vibrio cholerae serotype O1

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane both PBPb-I domains are membrane-distal with the pockets oriented relatively upwards, and both PBPb-II domains are membrane-proximal with the pockets relatively downwards. The two C-terminal alpha8' helices serving as pre-transmembrane sequences at the membrane-proximal end of the structure locate adjacent to each one and can be connected to the subsequent transmembrane helices Vibrio cholerae serotype O1 16020
-
additional information the periplasmic portion comprises residues 46-491. The periplasmic portion of CdgH forms a dimer in solution, L-arginine binding causes conformational changes of the dimer, structure overview. The architecture of the periplasmic tandem PBPb domains of CdgH may undergo a conformational changes from loose dimer to compact dimer Vibrio cholerae serotype O1
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
22300
-
 monomeric PBPbI domain, analytical ultracentrifugation Vibrio cholerae serotype O1
23100
-
 monomeric PBPbI domain, sequence calculation Vibrio cholerae serotype O1
87300
-
 recombinant dimeric periplasmic portion of enzyme CdgH, analytical ultracentrifugation Vibrio cholerae serotype O1
101600
-
 dimeric periplasmic portion of enzyme CdgH, sequence calculation Vibrio cholerae serotype O1

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 GTP Vibrio cholerae serotype O1
-
 2 diphosphate + cyclic di-3',5'-guanylate
-
 ?
2 GTP Vibrio cholerae serotype O1 El Tor Inaba N16961
-
 2 diphosphate + cyclic di-3',5'-guanylate
-
 ?
2 GTP Vibrio cholerae serotype O1 ATCC 39315
-
 2 diphosphate + cyclic di-3',5'-guanylate
-
 ?

Organism

Organism UniProt Comment Textmining
Vibrio cholerae serotype O1 Q9KT38
-
-
Vibrio cholerae serotype O1 ATCC 39315 Q9KT38
-
-
Vibrio cholerae serotype O1 El Tor Inaba N16961 Q9KT38
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant C-terminally His6-tagged CdgH periplasmic portion Vibrio cholerae serotype O1

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 GTP
-
 Vibrio cholerae serotype O1 2 diphosphate + cyclic di-3',5'-guanylate
-
 ?
2 GTP
-
 Vibrio cholerae serotype O1 El Tor Inaba N16961 2 diphosphate + cyclic di-3',5'-guanylate
-
 ?
2 GTP
-
 Vibrio cholerae serotype O1 ATCC 39315 2 diphosphate + cyclic di-3',5'-guanylate
-
 ?

Subunits

Subunits Comment Organism
More the periplasmic portion of CdgH forms a type I homodimer in solution which undergoes conformational changes upon L-arginine binding. The dimerization mode requires both tandem PBPb domains. Homodimerization leads to alignment of the two GGDEF domains, resulting in 2fold symmetry that enables the enzyme to catalyze c-diGMP synthesis Vibrio cholerae serotype O1

Synonyms

Synonyms Comment Organism
CdgH
-
 Vibrio cholerae serotype O1
DGC
-
 Vibrio cholerae serotype O1
GGDEF domain-containing protein UniProt Vibrio cholerae serotype O1
VC_1067
-
 Vibrio cholerae serotype O1

General Information

General Information Comment Organism
evolution proteins with a conserved C-terminal GGDEF domain act as DGCs, whereas proteins containing EAL or HD-GYP domains act as c-di-GMP-specific phosphodiesterases (PDEs). Vibrio cholerae genome typically encodes 31 proteins with a GGDEF domain Vibrio cholerae serotype O1
additional information the periplasmic portion of CdgH forms a homodimer in solution which undergoes conformational changes upon L-arginine binding. Homodimerization leads to alignment of the two GGDEF domains, resulting in 2fold symmetry that enables the enzyme to catalyze c-diGMP synthesis. Both tandem PBPb domains of CdgH contain a typical interlobe ligand-binding structural architecture. PBPb-I and -II domains have different amino acid binding specificity. The PBPb-I domain is primarily an L-arginine/L-lysine/L-ornithine-binding domain, whereas the PBPb-II domain exhibits a preference for L-glutamine and L-histidine, binding site structures, overview. Comparison of the CdgH PBPb-I domain with other amino acid-binding proteins Vibrio cholerae serotype O1
physiological function 3',5'-cyclic diguanylate monophosphate (c-di-GMP) is a ubiquitous secondary messenger that plays a key role in response regulation and lifestyle conventions of pathogenic bacteria, including Vibrio cholerae. Increases in c-di-GMP levels induce increased expression of various factors necessary for the establishment and maintenance of biofilm communities, whereas decreased levels usually lead to enhanced expression of virulence and motility factors related to biofilm degradation. C-di-GMP is synthesized from guanosine triphosphate by diguanylate cyclase (DGC) enzymes Vibrio cholerae serotype O1