› 3hq4

X-ray diffraction
2.2Å resolution

Crystal Structure of C151S mutant of Glyceraldehyde-3-phosphate dehydrogenase 1 (GAPDH1) complexed with NAD from Staphylococcus aureus MRSA252 at 2.2 angstrom resolution

Released:
DOI: 10.2210/pdb3hq4/pdb
PDB entry 3hq4 coloured by chain, front view.
PDB entry 3hq4 coloured by chain, side view.
PDB entry 3hq4 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: 36.3 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
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P21
Unit cell:
a: 68.671Å b: 105.92Å c: 91.374Å
α: 90° β: 108° γ: 90°
R-values:
R R work R free
0.187 0.184 0.244
Expression system: Escherichia coli

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Citations

1 review citation

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

2 mentions without citation

Identification of Alternative Allosteric Sites in Glycolytic Enzymes for Potential Use as Species-Specific Drug Targets.
Ayyildiz et al. (2020)
1 more