› 3fvm

X-ray diffraction
2.9Å resolution

Crystal structure of Steptococcus suis mannonate dehydratase with metal Mn++

Released:
DOI: 10.2210/pdb3fvm/pdb
PDB entry 3fvm coloured by chain, front view.
PDB entry 3fvm coloured by chain, side view.
PDB entry 3fvm coloured by chain, top view.
Source organism: Streptococcus suis
Primary publication:
Crystal structures of Streptococcus suis mannonate dehydratase (ManD) and its complex with substrate: genetic and biochemical evidence for a catalytic mechanism.
Zhang Q, Gao F, Peng H, Cheng H, Liu Y, Tang J, Thompson J, Wei G, Zhang J, Du Y, Yan J, Gao GF
J Bacteriol 191 5832-7 (2009)
PMID: 19617363

Function and Biology Details

Reaction catalysed: 
D-mannonate = 2-dehydro-3-deoxy-D-gluconate + H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-107453 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mannonate dehydratase Chains: A, B
Molecule details ›
Chains: A, B
Length: 386 amino acids
Theoretical weight: 43.02 KDa
Source organism: Streptococcus suis
Expression system: Escherichia coli
UniProt:
  • Canonical: A4VVI4 (Residues: 1-366; Coverage: 100%)
Gene names: SSU05_1157, uxuA
Sequence domains: D-mannonate dehydratase (UxuA)
Structure domains: Divalent-metal-dependent TIM barrel enzymes

Ligands and Environments

1 bound ligand:
Ligand MN 1 x MN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P43212
Unit cell:
a: 105.69Å b: 105.69Å c: 159.572Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.28 0.234 0.286
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Uncovering newly emerging variants of Streptococcus suis, an important zoonotic agent.
Feng et al. (2010)
7 other articles

1 mention without citation

Crystal structures of Streptococcus suis mannonate dehydratase (ManD) and its complex with substrate: genetic and biochemical evidence for a catalytic mechanism.
Zhang et al. (2009)