Crystal Structures of Group B Streptococcus Glyceraldehyde-3-Phosphate Dehydrogenase: Apo-Form, Binary and Ternary Complexes

Schormann, Norbert; Ayres, Chapelle A.; Fry, Alexandra; Green, Todd J.; Banerjee, Surajit; Ulett, Glen C.; Chattopadhyay, Debasish; Wlodawer, Alexander

doi:10.1371/journal.pone.0165917

Crystal Structures of Group B Streptococcus Glyceraldehyde-3-Phosphate Dehydrogenase: Apo-Form, Binary and Ternary Complexes

Journal Article · Tue Nov 22 00:00:00 EST 2016 · PLoS ONE

DOI:https://doi.org/10.1371/journal.pone.0165917· OSTI ID:1333943

Schormann, Norbert ^[1]; Ayres, Chapelle A. ^[1]; Fry, Alexandra ^[1]; Green, Todd J. ^[1]; Banerjee, Surajit ^[2]; Ulett, Glen C. ^[3]; ^[1]; Wlodawer, Alexander ^[4]

Univ. of Alabama, Birmingham, AL (United States)
Cornell Univ., Argonne, IL (United States)
Griffith Univ., Parklands (Australia)
National Cancer Inst., Frederick, MD (United States)

Glyceraldehyde 3-phosphate dehydrogenase or GAPDH is an evolutionarily conserved glycolytic enzyme. It catalyzes the two step oxidative phosphorylation of D-glyceraldehyde 3-phosphate into 1,3-bisphosphoglycerate using inorganic phosphate and NAD⁺ as cofactor. GAPDH of Group B Streptococcus is a major virulence factor and a potential vaccine candidate. Moreover, since GAPDH activity is essential for bacterial growth it may serve as a possible drug target. Crystal structures of Group B Streptococcus GAPDH in the apo-form, two different binary complexes and the ternary complex are described here. The two binary complexes contained NAD⁺ bound to 2 (mixed-holo) or 4 (holo) subunits of the tetrameric protein. The structure of the mixed-holo complex reveals the effects of NAD⁺ binding on the conformation of the protein. In the ternary complex, the phosphate group of the substrate was bound to the new Pi site in all four subunits. Comparison with the structure of human GAPDH showed several differences near the adenosyl binding pocket in Group B Streptococcus GAPDH. The structures also reveal at least three surface-exposed areas that differ in amino acid sequence compared to the corresponding areas of human GAPDH.

View Accepted Manuscript (DOE)

Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States)

Sponsoring Organization:: NIH-ORIP HEI; National Inst. of General Medical Sciences; USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22). Scientific User Facilities Division

Grant/Contract Number:: AC02-06CH11357; AC02-76SF00515

OSTI ID:: 1333943

Journal Information:: PLoS ONE, Journal Name: PLoS ONE Journal Issue: 11 Vol. 11; ISSN 1932-6203

Publisher:: Public Library of ScienceCopyright Statement

Country of Publication:: United States

Language:: ENGLISH

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Crystal Structures of Group B Streptococcus Glyceraldehyde-3-Phosphate Dehydrogenase: Apo-Form, Binary and Ternary Complexes

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