2bh2

From Proteopedia

Revision as of 10:16, 30 October 2007

CRYSTAL STRUCTURE OF E. COLI 5-METHYLURIDINE METHYLTRANSFERASE RUMA IN COMPLEX WITH RIBOSOMAL RNA SUBSTRATE AND S-ADENOSYLHOMOCYSTEINE.

Overview

A single base (U1939) within E. coli 23S ribosomal RNA is methylated by, its dedicated enzyme, RumA. The structure of, RumA/RNA/S-adenosylhomocysteine uncovers the mechanism for achieving, unique selectivity. The single-stranded substrate is "refolded" on the, enzyme into a compact conformation with six key intra-RNA interactions., The RNA substrate contributes directly to catalysis. In addition to the, target base, a second base is "flipped out" from the core loop to stack, against the adenine of the cofactor S-adenosylhomocysteine. Nucleotides in, permuted sequence order are stacked into the site vacated by the everted, target U1939 and compensate for the energetic penalty of base eversion., The 3' hairpin segment of the RNA binds distal to the active site and, provides binding energy ... [(full description)]

About this Structure

2BH2 is a [Single protein] structure of sequence from [Escherichia coli] with SAH and SF4 as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

A unique RNA Fold in the RumA-RNA-cofactor ternary complex contributes to substrate selectivity and enzymatic function., Lee TT, Agarwalla S, Stroud RM, Cell. 2005 Mar 11;120(5):599-611. PMID:15766524

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