1FZT

SOLUTION STRUCTURE AND DYNAMICS OF AN OPEN B-SHEET, GLYCOLYTIC ENZYME-MONOMERIC 23.7 KDA PHOSPHOGLYCERATE MUTASE FROM SCHIZOSACCHAROMYCES POMBE

1FZT の概要

• エントリーDOI: 10.2210/pdb1fzt/pdb
• 関連するPDBエントリー: 3PGM 4pgm 5pgm
• NMR情報: BMRB: 4648
• 分子名称: PHOSPHOGLYCERATE MUTASE (1 entity in total)
• 機能のキーワード: open b-sheet-helices, isomerase
• 由来する生物種: Schizosaccharomyces pombe (fission yeast)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23800.14

構造登録者

Uhrinova, S.,Uhrin, D.,Nairn, J.,Price, N.C.,Fothergill-Gilmore, L.A. (登録日: 2000-10-04, 公開日: 2001-03-14, 最終更新日: 2024-05-22)

主引用文献

Uhrinova, S.,Uhrin, D.,Nairn, J.,Price, N.C.,Fothergill-Gilmore, L.A.,Barlow, P.N.
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, 2001

PubMed 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.

PubMed: 11237600
DOI: 10.1006/jmbi.2000.4390

実験手法

SOLUTION NMR