3WJO

Crystal structure of Octaprenyl Pyrophosphate synthase from Escherichia coli with isopentenyl pyrophosphate (IPP)

3WJO の概要

• エントリーDOI: 10.2210/pdb3wjo/pdb
• 関連するPDBエントリー: 3WJK 3WJN
• 分子名称: Octaprenyl diphosphate synthase, 3-METHYLBUT-3-ENYL TRIHYDROGEN DIPHOSPHATE (3 entities in total)
• 機能のキーワード: prenyltransferase, site-directed mutagenesis, product chain length, transferase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 74431.57

構造登録者

Han, X.,Chen, C.C.,Kuo, C.J.,Huang, C.H.,Zheng, Y.,Ko, T.P.,Zhu, Z.,Feng, X.,Oldfield, E.,Liang, P.H.,Guo, R.T.,Ma, Y.H. (登録日: 2013-10-12, 公開日: 2014-06-18, 最終更新日: 2023-11-08)

主引用文献

Han, X.,Chen, C.C.,Kuo, C.J.,Huang, C.H.,Zheng, Y.,Ko, T.P.,Zhu, Z.,Feng, X.,Wang, K.,Oldfield, E.,Wang, A.H.,Liang, P.H.,Guo, R.T.,Ma, Y.
Crystal structures of ligand-bound octaprenyl pyrophosphate synthase from Escherichia coli reveal the catalytic and chain-length determining mechanisms.
Proteins, 83:37-45, 2015

PubMed Abstract: 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.

PubMed: 24895191
DOI: 10.1002/prot.24618

実験手法

X-RAY DIFFRACTION (2.45 Å)