PDBsum entry: 1fzt

Isomerase

PDB id: 1fzt

Contents

Protein chain

211 a.a. *

* Residue conservation analysis

PDB id:

1fzt

Name:

Isomerase

Title:

Solution structure and dynamics of an open b-sheet, glycolytic enzyme-monomeric 23.7 kda phosphoglycerate mutase from schizosaccharomyces pombe

Structure:

Phosphoglycerate mutase. Chain: a. Engineered: yes

Source:

Schizosaccharomyces pombe. Fission yeast. Organism_taxid: 4896. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932.

NMR struc:

21 models

Authors:

S.Uhrinova,D.Uhrin,J.Nairn,N.C.Price,L.A.Fothergill-Gilmore

Key ref:

S.Uhrínová et al. (2001). Solution structure and dynamics of an open beta-sheet, glycolytic enzyme, monomeric 23.7 kDa phosphoglycerate mutase from Schizosaccharomyces pombe. J Mol Biol, 306, 275-290. PubMed id: 11237600 DOI: 10.1006/jmbi.2000.4390

Date:

04-Oct-00 Release date: 14-Mar-01

Protein chain

P36623  (PMGY_SCHPO) -  Phosphoglycerate mutase

Seq: 211 a.a.

Struc: 211 a.a.

Enzyme reactions

• Enzyme class: E.C.5.4.2.1 - Phosphoglycerate mutase.
• Reaction: 2-phospho-D-glycerate = 3-phospho-D-glycerate

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 Gene Ontology (GO) functional annotation 

• Cellular component: nucleus (2 terms)
• Biological process: metabolic process (2 terms)
• Biochemical function: catalytic activity (4 terms)

Added reference

DOI no: 10.1006/jmbi.2000.4390

J Mol Biol 306:275-290 (2001)

PubMed id: 11237600

Solution structure and dynamics of an open beta-sheet, glycolytic enzyme, monomeric 23.7 kDa phosphoglycerate mutase from Schizosaccharomyces pombe.

S.Uhrínová, D.Uhrín, J.Nairn, N.C.Price, L.A.Fothergill-Gilmore, P.N.Barlow.

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 (3)J(HNHalpha) 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 A. The core of the enzyme includes an open, twisted, six-stranded beta-sheet flanked by four alpha-helices and a short 3(10)-helix. An additional smaller domain contains two short antiparallel beta-strands and a further pair of alpha-helices. The C(alpha) 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 A (0.92 A if only the beta-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. cerevisiae 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 fitted without invoking terms for fast internal motion or chemical exchange, and out of the remainder, 77 required a chemical exchange term. Significantly, 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 beta-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.

Selected figure(s)

Figure 3.
Figure 3. Summary of the inter-strand interactions observed for S. pombe PGAM. NOE connectivities are indicated by double-headed arrows; hydrogen bonds are indicated by double-headed arrows in boxes. (a) Central six-stranded β-sheet. (b) Small β-sheet formed by strands E and D.

Figure 5.
Figure 5. Structures of PGAMs from S. pombe and S. cerevisiae, shown as cartoon representations generated by MOLSCRIPT [Kraulis 1991]. (a) and (b) Structure of PGAM from S. pombe. (c) and (d) The 2.3 Å resolution X-ray structure of one subunit of tetrameric PGAM from S. cerevisiae. (b) and (d) The structures as in (a) and (c) but rotated by 90 ° around the y-axis. (e) Comparison of the active sites of monomeric PGAM from S. pombe (pink) and tetrameric PGAM from S. cerevisiae (green). The structures were aligned based on C^α atoms of residues 12–128, 132–202 from S. pombe PGAM and 5–121, 150–220 from S. cerevisiae PGAM.

The above figures are reprinted by permission from Elsevier: J Mol Biol (2001, 306, 275-290) copyright 2001.

Figures were selected by an automated process.