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TitleFunctionally critical residues in the aminoglycoside resistance-associated methyltransferase RmtC play distinct roles in 30S substrate recognition.
Journal, issue, pagesJ. Biol. Chem., Vol. 294, Page 17642-17653, Year 2019
Publish dateJul 8, 2019 (structure data deposition date)
AuthorsNosrati, M. / Dey, D. / Mehrani, A. / Strassler, S.E. / Zelinskaya, N. / Hoffer, E.D. / Stagg, S.M. / Dunham, C.M. / Conn, G.L.
External linksJ. Biol. Chem. / PubMed:31594862
MethodsX-ray diffraction
Resolution3.14 Å
Structure data

PDB-6pqb:
Crystal structure of aminoglycoside-resistance methyltransferase RmtC bound to S-adenosylhomocysteine (SAH)
Method: X-RAY DIFFRACTION / Resolution: 3.14 Å

Chemicals

ChemComp-SAH:
S-ADENOSYL-L-HOMOCYSTEINE

ChemComp-HOH:
WATER

Source
  • proteus mirabilis (bacteria)
KeywordsTRANSFERASE / methyltransferase / ribosome / aminoglycoside resistance / S-adenosylhomocysteine

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