1A4E

CATALASE A FROM SACCHAROMYCES CEREVISIAE

1A4E の概要

• エントリーDOI: 10.2210/pdb1a4e/pdb
• 分子名称: CATALASE A, AZIDE ION, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: oxidoreductase, catalase, peroxidase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Peroxisome: P15202
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 225321.87

構造登録者

Mate, M.J. (登録日: 1998-01-29, 公開日: 1999-08-13, 最終更新日: 2024-05-22)

主引用文献

Mate, M.J.,Zamocky, M.,Nykyri, L.M.,Herzog, C.,Alzari, P.M.,Betzel, C.,Koller, F.,Fita, I.
Structure of catalase-A from Saccharomyces cerevisiae.
J.Mol.Biol., 286:135-149, 1999

PubMed Abstract: The structure of the peroxisomal catalase A from the budding yeast Saccharomyces cerevisiae, with 515 residues per subunit, has been determined and refined to 2.4 A resolution. The crystallographic agreement factors R and Rfree are 15.4% and 19.8%, respectively. A tetramer with accurate 222-molecular symmetry is located in the asymmetric unit of the crystal. The conformation of the central core of catalase A, about 300 residues, remains similar to the structure of catalases from distantly related organisms. In contrast, catalase A lacks a carboxy-terminal domain equivalent to that found in catalase from Penicillium vitalae, the only other fungal catalase structure available. Structural peculiarities related with the heme and NADP(H) binding pockets can be correlated with biochemical characteristics of the catalase A enzyme. The network of molecular cavities and channels, filled with solvent molecules, supports the existence of one major substrate entry and at least two possible alternative pathways to the heme active site. The structure of the variant protein Val111Ala, also determined by X-ray crystallography at 2.8 A resolution, shows a few, well-localized, differences with respect to the wild-type enzyme. These differences, that include the widening of the entry channel in its narrowest point, provide an explanation for both the increased peroxidatic activity and the reduced catalatic activity of this mutant.

PubMed: 9931255
DOI: 10.1006/jmbi.1998.2453

実験手法

X-RAY DIFFRACTION (2.4 Å)