Structure of D-lactate dehydrogenase from Aquifex aeolicus complexed with NAD+ and lactic acid (or pyruvate)

被引：21

作者：

Antonyuk, Svetlana V. ^{[1
]}

Strange, Richard W. ^{[1
]}

Ellis, Mark J. ^{[2
]}

Bessho, Yoshitaka ^{[3
,4
]}

Kuramitsu, Seiki ^{[4
,5
]}

Inoue, Yumiko ^{[4
]}

Yokoyama, Shigeyuki ^{[3
,4
,6
]}

Hasnain, S. Samar ^{[1
]}

机构：

[1] Univ Liverpool, Mol Biophys Grp, Sch Biol Sci, Liverpool L69 7ZB, Merseyside, England

[2] STFC Daresbury Lab, Warrington WA4 4AD, Cheshire, England

[3] RIKEN, Yokohama Inst, Syst & Struct Biol Ctr, Yokohama, Kanagawa 2300045, Japan

[4] RIKEN SPring 8 Ctr, Harima Inst, Sayo, Hyogo 6795148, Japan

[5] Osaka Univ, Dept Biol Sci, Grad Sch Sci, Osaka 5600043, Japan

[6] Univ Tokyo, Dept Biophys & Biochem, Grad Sch Sci, Bunkyo Ku, Tokyo 1130033, Japan

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2009年 / 65卷

基金：

英国生物技术与生命科学研究理事会;

关键词：

FORMATE DEHYDROGENASE;

D O I：

10.1107/S1744309109044935

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The crystal structure of D-lactate dehydrogenase from Aquifex aeolicus (aq_727) was determined to 2.12 angstrom resolution in space group P2(1)2(1)2(1), with unit-cell parameters a = 90.94, b = 94.43, c = 188.85 angstrom. The structure was solved by molecular replacement using the coenzyme-binding domain of Lactobacillus helveticus D-lactate dehydrogenase and contained two homodimers in the asymmetric unit. Each subunit of the homodimer was found to be in a 'closed' conformation with the NADH cofactor bound to the coenzyme-binding domain and with a lactate (or pyruvate) molecule bound at the interdomain active-site cleft.

引用

页码：1209 / 1213

页数：5

共 17 条

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