4QX6: Crystal Structure Of Glyceraldehyde-3-phosphate Dehydrogenase From Streptococcus Agalactiae Nem316 At 2.46 Angstrom Resolution

Citation:
Abstract
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a conserved cytosolic enzyme, which plays a key role in glycolysis. GAPDH catalyzes the oxidative phosphorylation of D-glyceraldehyde 3-phosphate using NAD or NADP as a cofactor. In addition, GAPDH localized on the surface of some bacteria is thought to be involved in macromolecular interactions and bacterial pathogenesis. GAPDH on the surface of group B streptococcus (GBS) enhances bacterial virulence and is a potential vaccine candidate. Here, the crystal structure of GBS GAPDH from Streptococcus agalactiae in complex with NAD is reported at 2.46 A resolution. Although the overall structure of GBS GAPDH is very similar to those of other GAPDHs, the crystal structure reveals a significant difference in the area spanning residues 294-307, which appears to be more acidic. The amino-acid sequence of this region of GBS GAPDH is also distinct compared with other GAPDHs. This region therefore may be of interest as an immunogen for vaccine development.
PDB ID: 4QX6Download
MMDB ID: 123853
PDB Deposition Date: 2014/7/18
Updated in MMDB: 2014/10
Experimental Method:
x-ray diffraction
Resolution: 2.46  Å
Source Organism:
Similar Structures:
Biological Unit for 4QX6: tetrameric; determined by author and by software (PISA)
Molecular Components in 4QX6
Label Count Molecule
Proteins (4 molecules)
4
Glyceraldehyde 3-phosphate Dehydrogenase
Molecule annotation
Chemicals (6 molecules)
1
4
2
2
* Click molecule labels to explore molecular sequence information.

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