3RF9

X-ray structure of RlmN from Escherichia coli

Summary for 3RF9

• Entry DOI: 10.2210/pdb3rf9/pdb
• Related: 3RFA
• Descriptor: Ribosomal RNA large subunit methyltransferase N, IRON/SULFUR CLUSTER, (4R)-2-METHYLPENTANE-2,4-DIOL, ... (4 entities in total)
• Functional Keywords: radical sam, s-adenosylmethionine, iron sulfur cluster, methyltransferase, oxidoreductase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm : P36979
• Total number of polymer chains: 2
• Total formula weight: 91451.09

Authors

Boal, A.K.,Grove, T.L.,McLaughlin, M.I.,Yennawar, N.,Booker, S.J.,Rosenzweig, A.C. (deposition date: 2011-04-05, release date: 2011-05-11, Last modification date: 2024-02-21)

Primary citation

Boal, A.K.,Grove, T.L.,McLaughlin, M.I.,Yennawar, N.H.,Booker, S.J.,Rosenzweig, A.C.
Structural basis for methyl transfer by a radical SAM enzyme.
Science, 332:1089-1092, 2011

PubMed Abstract: The radical S-adenosyl-L-methionine (SAM) enzymes RlmN and Cfr methylate 23S ribosomal RNA, modifying the C2 or C8 position of adenosine 2503. The methyl groups are installed by a two-step sequence involving initial methylation of a conserved Cys residue (RlmN Cys(355)) by SAM. Methyl transfer to the substrate requires reductive cleavage of a second equivalent of SAM. Crystal structures of RlmN and RlmN with SAM show that a single molecule of SAM coordinates the [4Fe-4S] cluster. Residue Cys(355) is S-methylated and located proximal to the SAM methyl group, suggesting the SAM that is involved in the initial methyl transfer binds at the same site. Thus, RlmN accomplishes its complex reaction with structural economy, harnessing the two most important reactivities of SAM within a single site.

PubMed: 21527678
DOI: 10.1126/science.1205358

Experimental method

X-RAY DIFFRACTION (2.2 Å)