1I9G
CRYSTAL STRUCTURE OF AN ADOMET DEPENDENT METHYLTRANSFERASE
Summary for 1I9G
| Entry DOI | 10.2210/pdb1i9g/pdb |
| Descriptor | HYPOTHETICAL PROTEIN RV2118C, S-ADENOSYLMETHIONINE (3 entities in total) |
| Functional Keywords | mycobacterium, mtase, adomet, crystal, structural genomics, psi, protein structure initiative, tb structural genomics consortium, tbsgc, transferase |
| Biological source | Mycobacterium tuberculosis |
| Total number of polymer chains | 1 |
| Total formula weight | 30558.94 |
| Authors | Gupta, A.,Kumar, P.H.,Dineshkumar, T.K.,Varshney, U.,Subramanya, H.S.,TB Structural Genomics Consortium (TBSGC) (deposition date: 2001-03-20, release date: 2001-09-26, Last modification date: 2024-03-13) |
| Primary citation | Gupta, A.,Kumar, P.H.,Dineshkumar, T.K.,Varshney, U.,Subramanya, H.S. Crystal structure of Rv2118c: an AdoMet-dependent methyltransferase from Mycobacterium tuberculosis H37Rv. J.Mol.Biol., 312:381-391, 2001 Cited by PubMed Abstract: 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. PubMed: 11554794DOI: 10.1006/jmbi.2001.4935 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.98 Å) |
Structure validation
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