2fpo

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spinqualitylabelsall models 2fpo, resolution 2.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Putative methyltransferase yhhF from Escherichia coli.

Overview

N(2)-Methylguanine 966 is located in the loop of Escherichia coli 16 S, rRNA helix 31, forming a part of the P-site tRNA-binding pocket. We found, yhhF to be a gene encoding for m(2)G966 specific 16 S rRNA, methyltransferase. Disruption of the yhhF gene by kanamycin resistance, marker leads to a loss of modification at G966. The modification could be, rescued by expression of recombinant protein from the plasmid carrying the, yhhF gene. Moreover, purified m(2)G966 methyltransferase, in the presence, of S-adenosylomethionine (AdoMet), is able to methylate 30 S ribosomal, subunits that were purified from yhhF knock-out strain in vitro. The, methylation is specific for G966 base of the 16 S rRNA. The m(2)G966, methyltransferase was crystallized, and its structure has been determined, and refined to 2.05A(.) The structure closely resembles RsmC rRNA, methyltransferase, specific for m(2)G1207 of the 16 S rRNA. Structural, comparisons and analysis of the enzyme active site suggest modes for, binding AdoMet and rRNA to m(2)G966 methyltransferase. Based on the, experimental data and current nomenclature the protein expressed from the, yhhF gene was renamed to RsmD. A model for interaction of RsmD with, ribosome has been proposed.

About this Structure

2FPO is a Single protein structure of sequence from Escherichia coli with and as ligands. Full crystallographic information is available from OCA.

Reference

Methyltransferase that modifies guanine 966 of the 16 S rRNA: functional identification and tertiary structure., Lesnyak DV, Osipiuk J, Skarina T, Sergiev PV, Bogdanov AA, Edwards A, Savchenko A, Joachimiak A, Dontsova OA, J Biol Chem. 2007 Feb 23;282(8):5880-7. Epub 2006 Dec 21. PMID:17189261

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