› 3ksz

X-ray diffraction
2.6Å resolution

Crystal Structure of C151S+H178N mutant of Glyceraldehyde-3-phosphate-dehydrogenase 1 (GAPDH 1) from Staphylococcus aureus MRSA252 complexed with NAD and G3P

Released:
DOI: 10.2210/pdb3ksz/pdb
Model geometry
Fit model/data
PDB entry 3ksz coloured by chain, front view.
PDB entry 3ksz coloured by chain, side view.
PDB entry 3ksz 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: 36.28 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
1 bound ligand:
Ligand 3PG 4 x 3PG
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P21
Unit cell:
a: 67.872Å b: 93.596Å c: 89.884Å
α: 90° β: 107.61° γ: 90°
R-values:
R R work R free
0.203 0.2 0.248
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)
25 other articles