Structure of Streptococcus agalactiae glyceraldehyde-3-phosphate dehydrogenase holoenzyme reveals a novel surface.
Publication Type:Journal Article
Source:Acta Crystallogr F Struct Biol Commun, Volume 70, Issue Pt 10, p.1333-9 (2014)
Keywords:Amino Acid Sequence, Bacterial Proteins, Catalytic Domain, Conserved Sequence, Crystallography, X-Ray, Glyceraldehyde-3-Phosphate Dehydrogenases, Models, Molecular, Molecular Sequence Data, NAD, Protein Binding, Protein Structure, Quaternary, Streptococcus agalactiae, Structural Homology, Protein, Surface Properties
<p>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.</p>