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dc.contributor.authorAyres, Chapelle A
dc.contributor.authorSchormann, Norbert
dc.contributor.authorSenkovich, Olga
dc.contributor.authorFry, Alexandra
dc.contributor.authorBanerjee, Surajit
dc.contributor.authorUlett, Glen C
dc.contributor.authorChattopadhyay, Debasish
dc.date.accessioned2017-05-03T15:29:41Z
dc.date.available2017-05-03T15:29:41Z
dc.date.issued2014
dc.identifier.issn2053-230X
dc.identifier.doi10.1107/S2053230X14019517
dc.identifier.urihttp://hdl.handle.net/10072/65419
dc.description.abstractGlyceraldehyde-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 Šresolution. 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.
dc.description.peerreviewedYes
dc.description.publicationstatusYes
dc.format.extent2425458 bytes
dc.format.mimetypeapplication/pdf
dc.languageEnglish
dc.language.isoeng
dc.publisherWiley-Blackwell
dc.publisher.placeUnited States
dc.relation.ispartofstudentpublicationN
dc.relation.ispartofpagefrom1333
dc.relation.ispartofpageto1339
dc.relation.ispartofissue10
dc.relation.ispartofjournalActa Crystallographica Section F
dc.relation.ispartofvolume70
dc.rights.retentionY
dc.subject.fieldofresearchMedical Bacteriology
dc.subject.fieldofresearchcode110801
dc.titleStructure of Streptococcus agalactiae glyceraldehyde-3-phosphate dehydrogenase holoenzyme reveals a novel surface
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.rights.copyright© 2014 International Union of Crystallography. Published by Blackwell Publishing Ltd. This is the author-manuscript version of this paper. Reproduced in accordance with the copyright policy of the publisher. Please refer to the journal's website for access to the definitive, published version.
gro.hasfulltextFull Text
gro.griffith.authorUlett, Glen C.


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