4PGM

SACCHAROMYCES CEREVISIAE PHOSPHOGLYCERATE MUTASE

4PGM の概要

• エントリーDOI: 10.2210/pdb4pgm/pdb
• 分子名称: PHOSPHOGLYCERATE MUTASE 1 (2 entities in total)
• 機能のキーワード: transferase (phosphoryl), glycolytic enzyme, isomerase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 110069.48

構造登録者

Rigden, D.J.,Alexeev, D.,Phillips, S.E.V.,Fothergill-Gilmore, L.A. (登録日: 1997-04-25, 公開日: 1997-10-29, 最終更新日: 2024-05-22)

主引用文献

Rigden, D.J.,Alexeev, D.,Phillips, S.E.,Fothergill-Gilmore, L.A.
The 2.3 A X-ray crystal structure of S. cerevisiae phosphoglycerate mutase.
J.Mol.Biol., 276:449-459, 1998

PubMed Abstract: The high resolution crystal structure of Saccharomyces cerevisiae phosphoglycerate mutase has been determined. This structure shows important differences from the lower resolution structure deposited in 1982. The crystal used to determine the new structure was of a different form, having spacegroup P2(1). The model was refined to a crystallographic R-factor of 18.9% and a free R-factor of 28.4% using all data between 25 and 2.3 A and employing a bulk solvent correction. The enzyme is a tetramer of identical, 246 amino acid subunits, whose structure is revealed to be a dimer of dimers, with four independent active sites located well away from the subunit contacts. Each subunit contains two domains, the larger with a typical nucleotide binding fold, although phosphoglycerate mutase has no physiological requirement to bind nucleotides. The catalytic-site histidine residues are no longer in a "clapping-hands" conformation, but more resemble the conformation seen in the distantly related enzymes prostatic acid phosphatase and fructose-2,6-bisphosphatase. However, the catalytic histidine residues in the mutase are found to be much closer to each other than in the phosphatase structures, perhaps due to the absence of bound ligands in the mutase crystal. An intricate web of H-bonds is found around the catalytic histidine residues, high-lighting residues probably important for maintaining their correct orientation and charge. The positions of certain other residues, including some found near the catalytic site and some lining the catalytic-site cleft, have been changed by the correction of registration errors between sequence and electron density in the original structure. Electron density was apparent for a portion of the functionally important C-terminal tail, which was absent from the earlier structure, showing it to adopt a mainly helical conformation.

PubMed: 9512715
DOI: 10.1006/jmbi.1997.1554

実験手法

X-RAY DIFFRACTION (2.3 Å)