Crystal structures of ligand‐bound octaprenyl pyrophosphate synthase from Escherichia coli reveal the catalytic and chain‐length determining mechanisms. Issue 1 (18th November 2014)

• Record Type: Journal Article
• Authors: Han, Xu; Chen, Chun‐Chi; Kuo, Chih‐Jung; Huang, Chun‐Hsiang; Zheng, Yingying; Ko, Tzu‐Ping; Zhu, Zhen; Feng, Xinxin; Wang, Ke; Oldfield, Eric; Wang, Andrew H.‐J.; Liang, Po‐Huang; Guo, Rey‐Ting; Ma, Yanhe
• Is Part Of: Proteins. Volume 83:Issue 1(2015)
• Page Start: 37
• Page End: 45
• Publication Date: 2014-11-18
• Subjects: Proteins -- Periodicals; Proteins -- Periodicals; 572.6
• DOI: 10.1002/prot.24618
• Languages: English
• ISSNs: 0887-3585

Abstract

<abstract abstract-type="main"> <title>ABSTRACT</title> <p>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 <italic>trans</italic>‐prenyltransferase class of proteins. The structures of OPPs from <italic>Escherichia coli</italic> were solved in the apo‐form as well as in complexes with IPP and a FPP <italic>thio</italic>‐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 <italic>trans</italic>‐prenyltransferase and provide new information on the mechanisms of catalysis and product chain elongation. Proteins 2015; 83:37–45. © 2014 Wiley Periodicals, Inc.</p> </abstract>