1i9g

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spinqualitylabelsall models PDB ID 1i9g Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
, resolution 1.98Å
Ligands:
Gene:	RV2118C (Mycobacterium tuberculosis)
Domains:	GCD14
Resources:	FirstGlance, OCA, PDBsum, JenaLib, RCSB
Coordinates:	save as pdb, mmCIF, xml

CRYSTAL STRUCTURE OF AN ADOMET DEPENDENT METHYLTRANSFERASE

Overview

Rv2118c belongs to the class of conserved hypothetical proteins from Mycobacterium tuberculosis H37Rv. The crystal structure of Rv2118c in complex with S-adenosyl-l-methionine (AdoMet) has been determined at 1.98 A resolution. The crystallographic asymmetric unit consists of a monomer, but symmetry-related subunits interact extensively, leading to a tetrameric structure. The structure of the monomer can be divided functionally into two domains: the larger catalytic C-terminal domain that binds the cofactor AdoMet and is involved in the transfer of methyl group from AdoMet to the substrate and a smaller N-terminal domain. The structure of the catalytic domain is very similar to that of other AdoMet-dependent methyltransferases. The N-terminal domain is primarily a beta-structure with a fold not found in other methyltransferases of known structure. Database searches reveal a conserved family of Rv2118c-like proteins from various organisms. Multiple sequence alignments show several regions of high sequence similarity (motifs) in this family of proteins. Structure analysis and homology to yeast Gcd14p suggest that Rv2118c could be an RNA methyltransferase, but further studies are required to establish its functional role conclusively. Copyright 12001 Academic Press.

About this Structure

1I9G is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

Reference

Crystal structure of Rv2118c: an AdoMet-dependent methyltransferase from Mycobacterium tuberculosis H37Rv., Gupta A, Kumar PH, Dineshkumar TK, Varshney U, Subramanya HS, J Mol Biol. 2001 Sep 14;312(2):381-91. PMID:11554794

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