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TitleStructural and Functional Analysis of an O-Methyltransferase from the trans-AT PKS biosynthesis pathway
Journal, issue, pagesTo Be Published
Publish dateSep 19, 2018 (structure data deposition date)
AuthorsJakob, R.P. / Felber, P. / Demyanenko, Y. / Delbart, F. / Maier, T.
External linksSearch PubMed
MethodsX-ray diffraction
Resolution1.9 Å
Structure data

PDB-6hp1:
Crystal Structure of the O-Methyltransferase from the trans-AT PKS multienzyme C0ZGQ3 of Brevibacillus brevis
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-6hp2:
Crystal Structure of the O-Methyltransferase from the trans-AT PKS multienzyme C0ZGQ3 of Brevibacillus brevis in complex with S-Adenosyl-L-homocysteine
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-EMC:
ETHYL MERCURY ION

ChemComp-HOH:
WATER

ChemComp-SAH:
S-ADENOSYL-L-HOMOCYSTEINE

Source
  • brevibacillus brevis (strain 47 / jcm 6285 / nbrc 100599) (bacteria)
KeywordsTRANSFERASE / Polyketide / PKS / natural product / biosynthesis

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