› 3kwe

X-ray diffraction
1.1Å resolution

Inactive truncation of the beta-carboxysomal gamma-Carbonic Anhydrase, CcmM, form 2

Released:
DOI: 10.2210/pdb3kwe/pdb
PDB entry 3kwe coloured by chain, front view.
PDB entry 3kwe coloured by chain, side view.
PDB entry 3kwe coloured by chain, top view.
Source organism: Thermosynechococcus vestitus BP-1
Primary publication:
Structural basis of the oxidative activation of the carboxysomal gamma-carbonic anhydrase, CcmM.
Peña KL, Castel SE, de Araujo C, Espie GS, Kimber MS
Proc Natl Acad Sci U S A 107 2455-60 (2010)
PMID: 20133749

Function and Biology Details

Reaction catalysed: 
H(2)CO(3) = CO(2) + H(2)O
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184088 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carboxysome assembly protein CcmM Chain: A
Molecule details ›
Chain: A
Length: 213 amino acids
Theoretical weight: 23.08 KDa
Source organism: Thermosynechococcus vestitus BP-1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8DKB5 (Residues: 1-193; Coverage: 30%)
Gene names: ccmM, tll0944
Structure domains: Hexapeptide repeat proteins

Ligands and Environments

4 bound ligands:
Ligand ZN 1 x ZN
Ligand CL 2 x CL
Ligand MG 1 x MG
Ligand HEZ 1 x HEZ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: R3
Unit cell:
a: 102.931Å b: 102.931Å c: 44.903Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.13 0.129 0.139
Expression system: Escherichia coli

Quick links

Citations

33 review citations

Frontiers, opportunities, and challenges in biochemical and chemical catalysis of CO2 fixation.
Appel et al. (2013)
32 more

2 mentions without citation

Structural basis of the oxidative activation of the carboxysomal gamma-carbonic anhydrase, CcmM.
Peña et al. (2010)
1 more