› 4zvf

X-ray diffraction
1.15Å resolution

Crystal structure of GGDEF domain of the E. coli DosC - form II (GTP-alpha-S-bound)

Released:
DOI: 10.2210/pdb4zvf/pdb
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Source organism: Escherichia coli K-12
Primary publication:
Structural analysis of an oxygen-regulated diguanylate cyclase.
Tarnawski M, Barends TR, Schlichting I
Acta Crystallogr D Biol Crystallogr 71 2158-77 (2015)
PMID: 26527135

Function and Biology Details

Reaction catalysed: 
2 GTP = 2 diphosphate + cyclic di-3',5'-guanylate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141975 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Diguanylate cyclase DosC Chain: A
Molecule details ›
Chain: A
Length: 172 amino acids
Theoretical weight: 19.9 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AA89 (Residues: 297-460; Coverage: 36%)
Gene names: JW5241, b1490, dgcO, dosC, yddV
Sequence domains: Diguanylate cyclase, GGDEF domain
Structure domains: Alpha-Beta Plaits

Ligands and Environments

3 bound ligands:
Ligand GAV 1 x GAV
Ligand CA 2 x CA
Ligand EDO 2 x EDO
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P21
Unit cell:
a: 28.5Å b: 52.53Å c: 50.93Å
α: 90° β: 106.08° γ: 90°
R-values:
R R work R free
0.139 0.138 0.165
Expression system: Escherichia coli

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Citations

5 review citations

C-di-GMP Synthesis: Structural Aspects of Evolution, Catalysis and Regulation.
Schirmer T. (2016)
4 more

1 mention without citation

The importance of conserved amino acids in heme-based globin-coupled diguanylate cyclases.
Wan et al. (2017)

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