5F8C
Rv2258c-unbound
Summary for 5F8C
| Entry DOI | 10.2210/pdb5f8c/pdb |
| Related | 5F8E 5F8F |
| Descriptor | Methyltransferase, GLYCEROL (3 entities in total) |
| Functional Keywords | methyltransferase, class i, sinefungin, s-adenosyl-l-homocysteine, transferase |
| Biological source | Mycobacterium tuberculosis H37Rv |
| Total number of polymer chains | 3 |
| Total formula weight | 121840.19 |
| Authors | |
| Primary citation | Im, H.N.,Kim, H.S.,An, D.R.,Jang, J.Y.,Kim, J.,Yoon, H.J.,Yang, J.K.,Suh, S.W. Crystal structure of Rv2258c from Mycobacterium tuberculosis H37Rv, an S-adenosyl-l-methionine-dependent methyltransferase J.Struct.Biol., 193:172-180, 2016 Cited by PubMed Abstract: The Mycobacterium tuberculosis Rv2258c protein is an S-adenosyl-L-methionine (SAM)-dependent methyltransferase (MTase). Here, we have determined its crystal structure in three forms: a ligand-unbound form, a binary complex with sinefungin (SFG), and a binary complex with S-adenosyl-L-homocysteine (SAH). The monomer structure of Rv2258c consists of two domains which are linked by a long α-helix. The N-terminal domain is essential for dimerization and the C-terminal domain has the Class I MTase fold. Rv2258c forms a homodimer in the crystal, with the N-terminal domains facing each other. It also exists as a homodimer in solution. A DALI structural similarity search with Rv2258c reveals that the overall structure of Rv2258c is very similar to small-molecule SAM-dependent MTases. Rv2258c interacts with the bound SFG (or SAH) in an extended conformation maintained by a network of hydrogen bonds and stacking interactions. Rv2258c has a relatively large hydrophobic cavity for binding of the methyl-accepting substrate, suggesting that bulky nonpolar molecules with aromatic rings might be targeted for methylation by Rv2258c in M. tuberculosis. However, the ligand-binding specificity and the biological role of Rv2258c remain to be elucidated due to high variability of the amino acid residues defining the substrate-binding site. PubMed: 26772148DOI: 10.1016/j.jsb.2016.01.002 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.83 Å) |
Structure validation
Download full validation report
