Please use this identifier to cite or link to this item: http://hdl.handle.net/1893/830
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dc.contributor.authorNairn, Jacqueline-
dc.contributor.authorUhrinova, Stanislava-
dc.contributor.authorUhrin, Dusan-
dc.contributor.authorPrice, Nicholas C-
dc.contributor.authorBarlow, Paul N-
dc.date.accessioned2017-09-20T23:44:58Z-
dc.date.issued2001-02-16-
dc.identifier.urihttp://hdl.handle.net/1893/830-
dc.description.abstractThe structure and backbone dynamics of a double labelled (15N,13C) monomeric, 23.7 kD phosphoglycerate mutase (PGAM) from Schizosaccharomyces pombe have been investigated in solution using NMR spectroscopy. A set of 3125 NOE-derived distance restraints, 148 restraints representing inferred hydrogen bonds and 149 values of 3JHNHa were used in the structure calculation. The mean rmsd from the average structure for all backbone atoms from residues 6-205 in the best 21 calculated structures was 0.59 AÊ . The core of the enzyme includes an open, twisted, six-stranded b-sheet ¯anked by four a-helices and a short 310-helix. An additional smaller domain contains two short antiparallel b-strands and a further pair of a-helices. The Ca atoms of the S. pombe PGAM may be superimposed on their equivalents in one of the four identical subunits of Saccharomyces cerevisiae PGAM with an rmsd of 1.34 AÊ (0.92 AÊ if only the b-sheet is considered). Small differences between the two structures are attributable partly to the deletion in the S. pombe sequence of a 25 residue loop involved in stabilising the S. cerevisciae tetramer. Analysis of 15N relaxation parameters indicates that PGAM tumbles isotropically with a rotational correlation time of 8.7 ns and displays a range of dynamic features. Of 178 residues analysed, only 77 could be ®tted without invoking terms for fast internal motion or chemical exchange, and out of the remainder, 77 required a chemical exchange term. Signi®cantly, 46 of the slowly exchanging (milli- to microsecond) residues lie in helices, and these account for two-thirds of all analysed helix residues. On the contrary, only one b-sheet residue required an exchange term. In contrast to other analyses of backbone dynamics reported previously, residues in slow exchange appeared to correlate with architectural features of the enzyme rather than congregating close to ligand binding sitesen_UK
dc.language.isoen-
dc.publisherElsevier-
dc.relationNairn J, Uhrinova S, Uhrin D, Price NC & Barlow PN (2001) Solution structure and dynamics of an open β-sheet, glycolytic enzyme, monomeric 23.7 kDa phosphoglycerate mutase from Schizosaccharomyces pombe, Journal of Molecular Biology, 306 (2), pp. 275-290.-
dc.rightsThe publisher does not allow this work to be made publicly available in this Repository. Please use the Request a Copy feature at the foot of the Repository record to request a copy directly from the author; you can only request a copy if you wish to use this work for your own research or private study.-
dc.subjectphosphoglycerate mutaseen_UK
dc.subjectNMRen_UK
dc.subjectstructureen_UK
dc.subjectdynamicsen_UK
dc.subjectproteinen_UK
dc.subject.lcshEnolase-
dc.subject.lcshSchizosaccharomyces pombe-
dc.titleSolution structure and dynamics of an open β-sheet, glycolytic enzyme, monomeric 23.7 kDa phosphoglycerate mutase from Schizosaccharomyces pombeen_UK
dc.typeJournal Articleen_UK
dc.rights.embargodate2071-02-16T00:00:00Z-
dc.rights.embargoreasonThe publisher does not allow this work to be made publicly available in this Repository therefore there is an embargo on the full text of the work.-
dc.identifier.doihttp://dx.doi.org/10.1006/jmbi.2000.4390-
dc.identifier.pmid11237600-
dc.citation.jtitleJournal of Molecular Biology-
dc.citation.issn0022-2836-
dc.citation.volume306-
dc.citation.issue2-
dc.citation.spage275-
dc.citation.epage290-
dc.citation.publicationstatusPublished-
dc.citation.peerreviewedRefereed-
dc.type.statusPublisher version (final published refereed version)-
dc.identifier.urlhttp://www.sciencedirect.com/science/journal/00222836-
dc.author.emailjn2@stir.ac.uk-
dc.citation.date26/02/2002-
dc.contributor.affiliationBiological and Environmental Sciences-
dc.contributor.affiliationUniversity of Edinburgh-
dc.contributor.affiliationUniversity of Edinburgh-
dc.contributor.affiliationUniversity of Stirling-
dc.contributor.affiliationUniversity of Edinburgh-
dc.rights.embargoterms2071-02-16-
dc.rights.embargoliftdate2071-02-16-
dc.identifier.isi000167192400012-
Appears in Collections:Biological and Environmental Sciences Journal Articles

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