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Structure paper

TitleMolecular basis for the broad substrate selectivity of a peptide prenyltransferase.
Journal, issue, pagesProc. Natl. Acad. Sci. U.S.A., Vol. 113, Page 14037-14042, Year 2016
Publish dateNov 4, 2016 (structure data deposition date)
AuthorsHao, Y. / Pierce, E. / Roe, D. / Morita, M. / McIntosh, J.A. / Agarwal, V. / Cheatham, T.E. / Schmidt, E.W. / Nair, S.K.
External linksProc. Natl. Acad. Sci. U.S.A. / PubMed:27872314
MethodsX-ray diffraction
Resolution1.8 - 2.22 Å
Structure data

PDB-5tty:
PagF prenyltransferase
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-5tu4:
PagF with Boc-Tyr and DMSPP
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-5tu5:
PagF prenyltransferase with Tyr-Tyr-Tyr and DMSPP
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-5tu6:
PagF prenyltransferase with cyclic[INPYLYP] and DMSPP
Method: X-RAY DIFFRACTION / Resolution: 2.22 Å

Chemicals

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-HOH:
WATER

ChemComp-DST:
DIMETHYLALLYL S-THIOLODIPHOSPHATE

ChemComp-MG:
Unknown entry

ChemComp-B1C:
N-(tert-butoxycarbonyl)-L-tyrosine

ChemComp-MET:
METHIONINE

Source
  • planktothrix agardhii nies-596 (bacteria)
  • synthetic construct (others)
KeywordsTRANSFERASE / RiPP / prenylation / ABBA fold

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