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Structure paper

TitleStructural basis for substrate flexibility of the O-methyltransferase MpaG' involved in mycophenolic acid biosynthesis.
Journal, issue, pagesProtein Sci., Vol. 33, Page e5144-e5144, Year 2024
Publish dateJan 10, 2024 (structure data deposition date)
AuthorsYou, C. / Pan, Y. / Liu, R. / Li, S. / Feng, Y.
External linksProtein Sci. / PubMed:39150221
MethodsX-ray diffraction
Resolution1.99 - 2.13 Å
Structure data

PDB-8xte:
Crystal structure of methyltransferase MpaG' in complex with SAH and FDHMP
Method: X-RAY DIFFRACTION / Resolution: 1.99 Å

PDB-8xtf:
Crystal structure of methyltransferase MpaG' in complex with SAH and FDHMP-3C
Method: X-RAY DIFFRACTION / Resolution: 2.13 Å

PDB-8xtg:
Crystal structure of methyltransferase MpaG' in complex with SAH and DMMPA
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-SAH:
S-ADENOSYL-L-HOMOCYSTEINE

PDB-1lwb:
Crystal structure of prokaryotic phospholipase A2 at atomic resolution

ChemComp-HOH:
WATER

PDB-1lwc:
CRYSTAL STRUCTURE OF M184V MUTANT HIV-1 REVERSE TRANSCRIPTASE IN COMPLEX WITH NEVIRAPINE

PDB-1lwd:
CRYSTAL STRUCTURE OF NADP-DEPENDENT ISOCITRATE DEHYDROGENASE FROM PORCINE HEART MITOCHONDRIA

Source
  • penicillium brevicompactum (fungus)
KeywordsBIOSYNTHETIC PROTEIN / methyltransferase / MpaG' / MPA biosynthesis

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