Crystal structures of ligand-bound octaprenyl pyrophosphate synthase from Escherichia coli reveal the catalytic and chain-length determining mechanisms

Xu Han, Chun Chi Chen, Chih Jung Kuo, Chun Hsiang Huang, Yingying Zheng, Tzu Ping Ko, Zhen Zhu, Xinxin Feng, Ke Wang, Eric Oldfield, Andrew H.J. Wang, Po Huang Liang, Rey Ting Guo, Yanhe Ma

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16 引文 斯高帕斯(Scopus)

摘要

Octaprenyl pyrophosphate synthase (OPPs) catalyzes consecutive condensation reactions of one allylic substrate farnesyl pyrophosphate (FPP) and five homoallylic substrate isopentenyl pyrophosphate (IPP) molecules to form a C40 long-chain product OPP, which serves as a side chain of ubiquinone and menaquinone. OPPs belongs to the trans-prenyltransferase class of proteins. The structures of OPPs from Escherichia coli were solved in the apo-form as well as in complexes with IPP and a FPP thio-analog, FsPP, at resolutions of 2.2-2.6 Å, and revealed the detailed interactions between the ligands and enzyme. At the bottom of the active-site tunnel, M123 and M135 act in concert to form a wall which determines the final chain length. These results represent the first ligand-bound crystal structures of a long-chain trans-prenyltransferase and provide new information on the mechanisms of catalysis and product chain elongation.

原文英語
頁(從 - 到)37-45
頁數9
期刊Proteins: Structure, Function and Bioinformatics
83
發行號1
DOIs
出版狀態已發佈 - 1月 2015
對外發佈

ASJC Scopus subject areas

  • 結構生物學
  • 生物化學
  • 分子生物學

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