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Structure paper

TitleStructural Basis for Control of Methylation Extent in Polyketide Synthase Metal-Dependent C -Methyltransferases.
Journal, issue, pagesAcs Chem. Biol., Vol. 17, Page 2088-2098, Year 2022
Publish dateMar 16, 2022 (structure data deposition date)
AuthorsLao, Y. / Skiba, M.A. / Chun, S.W. / Narayan, A.R.H. / Smith, J.L.
External linksAcs Chem. Biol. / PubMed:35594521
MethodsX-ray diffraction
Resolution2.09 - 2.6 Å
Structure data

PDB-7uch:
AprA Methyltransferase 1 - GNAT in complex with Mn2+ , SAM, and Di-methyl-malonate
Method: X-RAY DIFFRACTION / Resolution: 2.18 Å

PDB-7uci:
SxtA Methyltransferase and decarboxylase didomain in complex with Mn2+ and SAH
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-7ucl:
SxtA Methyltransferase variant F458H in complex with Mn2+ and malonate
Method: X-RAY DIFFRACTION / Resolution: 2.09 Å

Chemicals

ChemComp-MN:
Unknown entry

ChemComp-GOL:
GLYCEROL

ChemComp-MU6:
dimethylpropanedioic acid

ChemComp-SAH:
S-ADENOSYL-L-HOMOCYSTEINE

ChemComp-HOH:
WATER

ChemComp-MLI:
MALONATE ION

Source
  • moorena bouillonii (bacteria)
  • cylindrospermopsis raciborskii (bacteria)
KeywordsTRANSFERASE / polyketide synthase / Methyltransferase

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