› 3k9q

X-ray diffraction
2.5Å resolution

Crystal structure of C151G mutant of Glyceraldehyde 3-phosphate dehydrogenase 1 from Methicillin resistant Staphylococcus aureus (MRSA252) at 2.5 angstrom resolution

Released:
DOI: 10.2210/pdb3k9q/pdb
PDB entry 3k9q coloured by chain, front view.
PDB entry 3k9q coloured by chain, side view.
PDB entry 3k9q coloured by chain, top view.
Source organism: Staphylococcus aureus subsp. aureus MRSA252
Primary publication:
Crystal structure of glyceraldehyde-3-phosphate dehydrogenase 1 from methicillin-resistant Staphylococcus aureus MRSA252 provides novel insights into substrate binding and catalytic mechanism.
Mukherjee S, Dutta D, Saha B, Das AK
J Mol Biol 401 949-68 (2010)
PMID: 20620151

Function and Biology Details

Reaction catalysed: 
D-glyceraldehyde 3-phosphate + phosphate + NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-179681 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glyceraldehyde-3-phosphate dehydrogenase 1 Chains: O, P, Q, R
Molecule details ›
Chains: O, P, Q, R
Length: 336 amino acids
Theoretical weight: 36.27 KDa
Source organism: Staphylococcus aureus subsp. aureus MRSA252
Expression system: Escherichia coli
UniProt:
  • Canonical: Q6GIL8 (Residues: 1-336; Coverage: 100%)
Gene names: SAR0828, gap, gapA, gapA1
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 4 x NAD
2 bound ligands:
Ligand GOL 3 x GOL
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P21
Unit cell:
a: 67.933Å b: 105.142Å c: 90.76Å
α: 90° β: 107.48° γ: 90°
R-values:
R R work R free
0.185 0.183 0.231
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Redox regulation by reversible protein S-thiolation in Gram-positive bacteria.
Imber et al. (2019)
25 other articles

1 mention without citation

Direct assessment of histone function using histone replacement.
Corcoran et al. (2023)