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Structure of a phosphoglycerate mutase:3-phosphoglyceric acid complex at 1.7 A.

dc.contributor.authorCrowhurst, GS
dc.contributor.authorDalby, Andrew R
dc.contributor.authorIsupov, MN
dc.contributor.authorCampbell, JW
dc.contributor.authorLittlechild, JA
dc.date.accessioned2015-10-08T08:27:14Z
dc.date.issued1999-11
dc.description.abstractThe crystal structure of the tetrameric glycolytic enzyme phosphoglycerate mutase from the yeast Saccharomyces cerevisiae has been determined to 1.7 A resolution in complex with the sugar substrate. The difference map indicates that 3-phosphoglycerate is bound at the base of a 12 A cleft, positioning C2 of the substrate within 3.5 A of the primary catalytic residue, histidine 8.en_GB
dc.description.sponsorshipBBSRCen_GB
dc.identifier.citationActa Crystallographica, Vol. 55, pp. 1822 - 1826en_GB
dc.identifier.urihttp://hdl.handle.net/10871/18384
dc.language.isoenen_GB
dc.publisherInternational Union of Crystallographyen_GB
dc.relation.urlhttp://www.ncbi.nlm.nih.gov/pubmed/10531478en_GB
dc.relation.urlhttp://scripts.iucr.org/cgi-bin/paper?AD0081en_GB
dc.rights© 1999 International Union of Crystallographyen_GB
dc.subjectBinding Sitesen_GB
dc.subjectCrystallography, X-Rayen_GB
dc.subjectFungal Proteinsen_GB
dc.subjectGlyceric Acidsen_GB
dc.subjectHydrogen Bondingen_GB
dc.subjectModels, Molecularen_GB
dc.subjectPhosphoglycerate Mutaseen_GB
dc.subjectSaccharomyces cerevisiaeen_GB
dc.subjectSulfatesen_GB
dc.titleStructure of a phosphoglycerate mutase:3-phosphoglyceric acid complex at 1.7 A.en_GB
dc.typeArticleen_GB
dc.date.available2015-10-08T08:27:14Z
dc.identifier.issn0907-4449
exeter.place-of-publicationDENMARK
dc.descriptionJournal Articleen_GB
dc.descriptionResearch Support, Non-U.S. Gov'ten_GB
dc.identifier.journalActa Crystallographica Section D: Biological Crystallographyen_GB


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