2NX9

Crystal structure of the carboxyltransferase domain of the oxaloacetate decarboxylase Na+ pump from Vibrio cholerae

2NX9 の概要

• エントリーDOI: 10.2210/pdb2nx9/pdb
• 関連するPDBエントリー: 1RQH
• 分子名称: Oxaloacetate decarboxylase 2, subunit alpha, ZINC ION (3 entities in total)
• 機能のキーワード: oxaloacetate decarboxylase, carboxyltransferase structure, biotin enzymes, zn2+ binding site, tim-barrel fold, lyase
• 由来する生物種: Vibrio cholerae
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 103092.48

構造登録者

Studer, R.,Dimroth, P. (登録日: 2006-11-17, 公開日: 2006-12-26, 最終更新日: 2023-08-30)

主引用文献

Studer, R.,Dahinden, P.,Wang, W.W.,Auchli, Y.,Li, X.D.,Dimroth, P.
Crystal Structure of the Carboxyltransferase Domain of the Oxaloacetate Decarboxylase Na(+) Pump from Vibrio cholerae.
J.Mol.Biol., 367:547-557, 2007

PubMed Abstract: Oxaloacetate decarboxylase is a membrane-bound multiprotein complex that couples oxaloacetate decarboxylation to sodium ion transport across the membrane. The initial reaction catalyzed by this enzyme machinery is the carboxyl transfer from oxaloacetate to the prosthetic biotin group. The crystal structure of the carboxyltransferase at 1.7 A resolution shows a dimer of alpha(8)beta(8) barrels with an active site metal ion, identified spectroscopically as Zn(2+), at the bottom of a deep cleft. The enzyme is completely inactivated by specific mutagenesis of Asp17, His207 and His209, which serve as ligands for the Zn(2+) metal ion, or by Lys178 near the active site, suggesting that Zn(2+) as well as Lys178 are essential for the catalysis. In the present structure this lysine residue is hydrogen-bonded to Cys148. A potential role of Lys178 as initial acceptor of the carboxyl group from oxaloacetate is discussed.

PubMed: 17270211
DOI: 10.1016/j.jmb.2006.12.035

実験手法

X-RAY DIFFRACTION (1.7 Å)