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TitleTwo Distinct Substrate Binding Modes for the Normal and Reverse Prenylation of Hapalindoles by the Prenyltransferase AmbP3
Journal, issue, pagesAngew. Chem. Int. Ed. Engl., Vol. 57, Page 560-563, Year 2018
Publish dateAug 3, 2017 (structure data deposition date)
AuthorsWong, C.P. / Awakawa, T. / Nakashima, Y. / Mori, T. / Zhu, Q. / Liu, X. / Abe, I.
External linksAngew. Chem. Int. Ed. Engl. / PubMed:29178634
MethodsX-ray diffraction
Resolution1.65 - 2.003 Å
Structure data

PDB-5y4g:
Apo Structure of AmbP3
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-5y72:
DMSPP Bound AmbP3
Method: X-RAY DIFFRACTION / Resolution: 1.65 Å

PDB-5y7c:
Hapalindole A and DMSPP Bound AmbP3
Method: X-RAY DIFFRACTION / Resolution: 2.003 Å

PDB-5y84:
Hapalindole U and DMSPP Bound AmbP3
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-DST:
DIMETHYLALLYL S-THIOLODIPHOSPHATE

ChemComp-8O0:
Hapalindole A

ChemComp-8P6:
Hapalindole U

Source
  • fischerella ambigua utex 1903 (bacteria)
KeywordsTRANSFERASE / Prenyltransferase

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