Crystal structure of Rv2118c: an AdoMet-dependent methyltransferase from Mycobacterium tuberculosis H37Rv

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-...

Full description

Saved in:
Bibliographic Details
Published in:Journal of molecular biology 2001-09, Vol.312 (2), p.381-391
Main Authors: Gupta, A, Kumar, P H, Dineshkumar, T K, Varshney, U, Subramanya, H S
Format: Article
Language:English
Subjects:
Amino Acid Motifs
Amino Acid Sequence
Binding Sites
Catalytic Domain
Conserved Sequence
Crystallography, X-Ray
Fungal Proteins - chemistry
methyltransferase
Methyltransferases - chemistry
Methyltransferases - metabolism
Models, Molecular
Molecular Sequence Data
Mycobacterium tuberculosis
Mycobacterium tuberculosis - enzymology
Protein Structure, Quaternary
Protein Structure, Tertiary
Repressor Proteins - chemistry
Rv2118c protein
S-Adenosylmethionine - metabolism
Saccharomyces cerevisiae Proteins
Sequence Alignment
Static Electricity
tRNA Methyltransferases
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:0022-2836
1089-8638
DOI:10.1006/jmbi.2001.4935