期刊
JOURNAL OF STRUCTURAL BIOLOGY
卷 170, 期 1, 页码 76-82出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.jsb.2009.11.012
关键词
Protoporphyrinogen IX oxidase; Tetrapyrrole biosynthesis; BsPPO; Acifluorfen; Variegate porphyria
资金
- MOST [2007CB914301, 2009CB825504, 2006AA02A319, 2006AA020502, 2003CB114403, 2008DFA30770]
- TBR program [08QTPTJC28200, 08SYSYTC00200, 07JCYBJC19200]
- NSFC [30940015, 20432010, 90713011, 30770428]
- MOE [104189]
Protoporphyrinogen IX oxidase (PPO) converts protoporphyrinogen IX to protoporphyrin IX, playing an important part in the heme/chlorophyll biosynthetic pathway. Bacillus subtilis PPO (bsPPO) is unique among PPO family members in that it is a soluble monomer, is inefficiently inhibited by the herbicide acifluorfen (AF) and has broader substrate specificity than other PPO enzymes. Here, we present the crystal structure of bsPPO bound to AF. Our structure shows that the AF molecule binds to a new site outside the previously identified inhibitor binding pocket. Most importantly, the benzene ring of the 2-nitrobenzoic acid moiety of AF lies parallel to the isoalloxazine ring of FAD at a distance of less than 3.5 angstrom, providing a framework for the interaction of FAD with the substrate protoporphyrinogen IX. Furthermore, our structure reveals that the larger substrate binding chamber and predominantly positively charged chamber surface of bsPPO are more favorable or the binding of coproporphyrinogen-III. These crystallographic findings uncover biochemically unique properties of bsPPO, providing important information for further understanding the enzymatic mechanism. (C) 2009 Elsevier Inc. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据