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3WJO

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

Summary for 3WJO
Entry DOI10.2210/pdb3wjo/pdb
Related3WJK 3WJN
DescriptorOctaprenyl diphosphate synthase, 3-METHYLBUT-3-ENYL TRIHYDROGEN DIPHOSPHATE (3 entities in total)
Functional Keywordsprenyltransferase, site-directed mutagenesis, product chain length, transferase
Biological sourceEscherichia coli
Total number of polymer chains2
Total formula weight74431.57
Authors
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. (deposition date: 2013-10-12, release date: 2014-06-18, Last modification date: 2023-11-08)
Primary citationHan, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.45 Å)
Structure validation

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