1V5G

Crystal Structure of the Reaction Intermediate between Pyruvate oxidase containing FAD and TPP, and Substrate Pyruvate

1V5G の概要

• エントリーDOI: 10.2210/pdb1v5g/pdb
• 関連するPDBエントリー: 1POX 1V5E 1V5F
• 分子名称: Pyruvate oxidase, MAGNESIUM ION, FLAVIN-ADENINE DINUCLEOTIDE, ... (5 entities in total)
• 機能のキーワード: oxidoreductase, flavoprotein
• 由来する生物種: Aerococcus viridans
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 66513.62

構造登録者

Hossain, M.T.,Suzuki, K.,Yamamoto, T.,Imamura, S.,Sekiguchi, T.,Takenaka, A. (登録日: 2003-11-22, 公開日: 2005-06-28, 最終更新日: 2023-11-08)

主引用文献

Juan, E.C.,Hoque, M.M.,Hossain, M.T.,Yamamoto, T.,Imamura, S.,Suzuki, K.,Sekiguchi, T.,Takenaka, A.
The structures of pyruvate oxidase from Aerococcus viridans with cofactors and with a reaction intermediate reveal the flexibility of the active-site tunnel for catalysis.
Acta Crystallogr.,Sect.F, 63:900-907, 2007

PubMed Abstract: The crystal structures of pyruvate oxidase from Aerococcus viridans (AvPOX) complexed with flavin adenine dinucleotide (FAD), with FAD and thiamine diphosphate (ThDP) and with FAD and the 2-acetyl-ThDP intermediate (AcThDP) have been determined at 1.6, 1.8 and 1.9 A resolution, respectively. Each subunit of the homotetrameric AvPOX enzyme consists of three domains, as observed in other ThDP-dependent enzymes. FAD is bound within one subunit in the elongated conformation and with the flavin moiety being planar in the oxidized form, while ThDP is bound in a conserved V-conformation at the subunit-subunit interface. The structures reveal flexible regions in the active-site tunnel which may undergo conformational changes to allow the entrance of the substrates and the exit of the reaction products. Of particular interest is the role of Lys478, the side chain of which may be bent or extended depending on the stage of catalysis. The structures also provide insight into the routes for electron transfer to FAD and the involvement of active-site residues in the catalysis of pyruvate to its products.

PubMed: 18007037
DOI: 10.1107/S1744309107041012

実験手法

X-RAY DIFFRACTION (1.96 Å)