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TitleCrystal structures of ligand-bound octaprenyl pyrophosphate synthase from Escherichia coli reveal the catalytic and chain-length determining mechanisms.
Journal, issue, pagesProteins, Vol. 83, Page 37-45, Year 2015
Publish dateOct 11, 2013 (structure data deposition date)
AuthorsHan, X. / Chen, C.C. / Kuo, C.J. / Huang, C.H. / Zheng, Y. / Ko, T.P. / Zhu, Z. / Feng, X. / Wang, K. / Oldfield, E. ...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.
External linksProteins / PubMed:24895191
MethodsX-ray diffraction
Resolution2.2 - 2.6 Å
Structure data

PDB-3wjk:
Crystal structure of Octaprenyl Pyrophosphate synthase from Escherichia coli
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-3wjn:
Crystal structure of Octaprenyl Pyrophosphate synthase from Escherichia coli with farnesyl S-thiol-pyrophosphate (FSPP)
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-3wjo:
Crystal structure of Octaprenyl Pyrophosphate synthase from Escherichia coli with isopentenyl pyrophosphate (IPP)
Method: X-RAY DIFFRACTION / Resolution: 2.45 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-FPS:
S-[(2E,6E)-3,7,11-TRIMETHYLDODECA-2,6,10-TRIENYL] TRIHYDROGEN THIODIPHOSPHATE

ChemComp-IPE:
3-METHYLBUT-3-ENYL TRIHYDROGEN DIPHOSPHATE

Source
  • escherichia coli (E. coli)
KeywordsTRANSFERASE / prenyltransferase / site-directed mutagenesis / product chain length

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