Please use this identifier to cite or link to this item:
Appears in Collections:Biological and Environmental Sciences Journal Articles
Peer Review Status: Refereed
Title: Solution structure and dynamics of an open β-sheet, glycolytic enzyme, monomeric 23.7 kDa phosphoglycerate mutase from Schizosaccharomyces pombe
Authors: Nairn, Jacqueline
Uhrinova, Stanislava
Uhrin, Dusan
Price, Nicholas C
Barlow, Paul N
Contact Email:
Keywords: phosphoglycerate mutase
Issue Date: 16-Feb-2001
Publisher: Elsevier
Citation: Nairn 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.
Abstract: The 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 sites
Type: Journal Article
DOI Link:
Rights: The 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.
Affiliation: Biological and Environmental Sciences
University of Edinburgh
University of Edinburgh
University of Stirling
University of Edinburgh

Files in This Item:
File Description SizeFormat 
pombe solution structure.pdf609.51 kBAdobe PDFUnder Embargo until 16/2/2071     Request a copy

Note: If any of the files in this item are currently embargoed, you can request a copy directly from the author by clicking the padlock icon above. However, this facility is dependant on the depositor still being contactable at their original email address.

This item is protected by original copyright

Items in the Repository are protected by copyright, with all rights reserved, unless otherwise indicated.

If you believe that any material held in STORRE infringes copyright, please contact providing details and we will remove the Work from public display in STORRE and investigate your claim.