1POX

THE REFINED STRUCTURES OF A STABILIZED MUTANT AND OF WILD-TYPE PYRUVATE OXIDASE FROM LACTOBACILLUS PLANTARUM

1POX の概要

• エントリーDOI: 10.2210/pdb1pox/pdb
• 分子名称: PYRUVATE OXIDASE, MAGNESIUM ION, SODIUM ION, ... (7 entities in total)
• 機能のキーワード: oxidoreductase(oxygen as acceptor)
• 由来する生物種: Lactobacillus plantarum
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 131115.32

構造登録者

Muller, Y.A.,Schulz, G.E. (登録日: 1993-11-09, 公開日: 1994-01-31, 最終更新日: 2024-02-14)

主引用文献

Muller, Y.A.,Schumacher, G.,Rudolph, R.,Schulz, G.E.
The refined structures of a stabilized mutant and of wild-type pyruvate oxidase from Lactobacillus plantarum.
J.Mol.Biol., 237:315-335, 1994

PubMed Abstract: The crystal structure of pyruvate oxidase (EC 1.2.3.3) from Lactobacillus plantarum stabilized by three point mutations has been refined at 2.1 A resolution using the simulated annealing method. Based on 87,775 independent reflections in the resolution range 10 to 2.1 A, a final R-factor of 16.2% was obtained at good model geometry. The wild-type enzyme crystallizes isomorphously with the stabilized enzyme and has been analyzed at 2.5 A resolution. Pyruvate oxidase is a homotetramer with point group symmetry D2. One 2-fold axis is crystallographic, the others are local. The crystallographic asymmetric unit contains two subunits, and the model consists of the two polypeptide chains (residues 9 through 593), two FAD, two ThDP*Mg2+ and 739 water molecules. Each subunit has three domains; the CORE domain, the FAD domain and the ThDP domain. The FAD-binding chain fold is different from those of other known flavoproteins, whereas the ThDP-binding chain fold resembles the corresponding folds of the two other ThDP enzymes whose structure is known, transketolase and pyruvate decarboxylase. The peptide environment most likely forces the pyrimidine ring of ThDP into an unusual tautomeric form, which is required for catalysis. The structural differences between the wild-type and the stabilized enzyme are small. All three point mutations are at or near to the subunit interfaces, indicating that they stabilize the quarternary structure as had been deduced from reconstitution experiments.

PubMed: 8145244
DOI: 10.1006/jmbi.1994.1233

実験手法

X-RAY DIFFRACTION (2.1 Å)