4QX6

CRYSTAL STRUCTURE OF GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE FROM STREPTOCOCCUS AGALACTIAE NEM316 at 2.46 ANGSTROM RESOLUTION

Summary for 4QX6

• Entry DOI: 10.2210/pdb4qx6/pdb
• Related: 3K73
• Descriptor: Glyceraldehyde 3-phosphate dehydrogenase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: rossmann fold, nad, gapdh, oxidoreductase, glycolysis
• Biological source: Streptococcus agalactiae
• Total number of polymer chains: 4
• Total formula weight: 155637.30

Authors

Ayres, C.A.,Schormann, N.,Banerjee, S.,Chattopadhyay, D. (deposition date: 2014-07-18, release date: 2014-10-15, Last modification date: 2024-04-03)

Primary citation

Ayres, C.A.,Schormann, N.,Senkovich, O.,Fry, A.,Banerjee, S.,Ulett, G.C.,Chattopadhyay, D.
Structure of Streptococcus agalactiae glyceraldehyde-3-phosphate dehydrogenase holoenzyme reveals a novel surface.
Acta Crystallogr F Struct Biol Commun, 70:1333-1339, 2014

PubMed 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 Å 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.

PubMed: 25286935
DOI: 10.1107/S2053230X14019517

Experimental method

X-RAY DIFFRACTION (2.46 Å)