Structure of Streptococcus agalactiae glyceraldehyde‐3‐phosphate dehydrogenase holoenzyme reveals a novel surface. Issue 10 (1st October 2014)

• Record Type: Journal Article
• Authors: Ayres, Chapelle A.; Schormann, Norbert; Senkovich, Olga; Fry, Alexandra; Banerjee, Surajit; Ulett, Glen C.; Chattopadhyay, Debasish
• Is Part Of: Acta crystallographica. Volume 70:Issue 10(2014:Oct.)
• Page Start: 1333
• Page End: 1339
• Publication Date: 2014-10-01
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X14019517
• Languages: English
• ISSNs: 2053-230X

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <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 <italic>Streptococcus agalactiae</italic> 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> </abstract>