Crystal structure of L-sorbose dehydrogenase, a pyrroloquinoline quinone-dependent enzyme with homodimeric assembly, from Ketogulonicigenium vulgare

被引：19

作者：

Han, Xiaodong ^{[1
]}

Xiong, Xianghua ^{[2
]}

Jiang, Dunquan ^{[1
]}

Chen, Sihan ^{[1
]}

Huang, Enyu ^{[1
]}

Zhang, Weicai ^{[2
]}

Liu, Xinqi ^{[1
]}

机构：

[1] Nankai Univ, Coll Life Sci, State Key Lab Med Chem Biol, Tianjin 300071, Peoples R China

[2] Beijing Inst Biotechnol, Lab Microorganism Engn, Beijing 100071, Peoples R China

来源：

BIOTECHNOLOGY LETTERS | 2014年 / 36卷 / 05期

基金：

中国国家自然科学基金;

关键词：

Crystal structure; Cytochrome c551; 2-Keto-L-gulonic acid; Ketogulonicigenium vulgare; L-Sorbose dehydrogenase; Pyrroloquinoline quinone;

D O I：

10.1007/s10529-013-1446-5

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

The crystal structure of the l-sorbose dehydrogenase (SDH) from Ketogulonicigenium vulgare Y25 has been determined at 2.7 resolution using the molecular replacement method. The overall structure of SDH is similar to that of other quinoprotein dehydrogenases; consisting of an eight bladed beta-propeller PQQ domain and protrusion loops. We identified a stable homodimer in crystal and demonstrated its existence in solution by sedimentation velocity measurement. By biochemical characterization of the SDH in vitro, using l-sorbose as substrate and cytochrome c551 as electron acceptor, we revealed cytochrome c551 acting as physiological primary electron acceptor for SDH.

引用

页码：1001 / 1008

页数：8

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