1uwv

From Proteopedia

Revision as of 16:05, 18 December 2007

CRYSTAL STRUCTURE OF RUMA, THE IRON-SULFUR CLUSTER CONTAINING E. COLI 23S RIBOSOMAL RNA 5-METHYLURIDINE METHYLTRANSFERASE

Overview

RumA catalyzes transfer of a methyl group from S-adenosylmethionine (SAM), specifically to uridine 1939 of 23S ribosomal RNA in Escherichia coli to, yield 5-methyluridine. We determined the crystal structure of RumA at 1.95, A resolution. The protein is organized into three structural domains: The, N-terminal domain contains sequence homology to the conserved TRAM motif, and displays a five-stranded beta barrel architecture characteristic of an, oligosaccharide/oligonucleotide binding fold. The central domain contains, a [Fe(4)S(4)] cluster coordinated by four conserved cysteine residues. The, C-terminal domain displays the typical SAM-dependent methyltransferase, fold. The catalytic nucleophile Cys389 lies in a motif different from that, in DNA 5-methylcytosine methyltransferases. The electrostatic potential, surface reveals a predominately positively charged area that covers the, concave surface of the first two domains and suggests an RNA binding mode., The iron-sulfur cluster may be involved in the correct folding of the, protein or may have a role in RNA binding.

About this Structure

1UWV is a Single protein structure of sequence from Escherichia coli with NI, PO4, CL and SF4 as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Crystal structure of RumA, an iron-sulfur cluster containing E. coli ribosomal RNA 5-methyluridine methyltransferase., Lee TT, Agarwalla S, Stroud RM, Structure. 2004 Mar;12(3):397-407. PMID:15016356

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