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dc.contributor.authorSchormann, Norbert
dc.contributor.authorAyres, Chapelle A
dc.contributor.authorFry, Alexandra
dc.contributor.authorGreene, Todd J
dc.contributor.authorBanerjee, Surajit
dc.contributor.authorUlett, Glen C
dc.contributor.authorChattopadhyay, Debasish
dc.date.accessioned2018-01-19T06:21:09Z
dc.date.available2018-01-19T06:21:09Z
dc.date.issued2016
dc.identifier.issn1932-6203
dc.identifier.doi10.1371/journal.pone.0165917
dc.identifier.urihttp://hdl.handle.net/10072/101006
dc.description.abstractGlyceraldehyde 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.
dc.description.peerreviewedYes
dc.languageEnglish
dc.language.isoeng
dc.publisherPublic Library of Sciences
dc.relation.ispartofpagefrome0165917-1
dc.relation.ispartofpagetoe0165917-15
dc.relation.ispartofissue11
dc.relation.ispartofjournalPLoS One
dc.relation.ispartofvolume11
dc.subject.fieldofresearchMedical Bacteriology
dc.subject.fieldofresearchcode110801
dc.titleCrystal Structures of Group B Streptococcus Glyceraldehyde-3-Phosphate Dehydrogenase: Apo-Form, Binary and Ternary Complexes
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
dcterms.licensehttps://creativecommons.org/licenses/by/4.0/
dc.description.versionVersion of Record (VoR)
gro.rights.copyright© 2016 Schormann et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
gro.hasfulltextFull Text
gro.griffith.authorUlett, Glen C.


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