5F8E

Rv2258c-SAH

5F8E の概要

• エントリーDOI: 10.2210/pdb5f8e/pdb
• 関連するPDBエントリー: 5F8C 5F8F
• 分子名称: Methyltransferase, S-ADENOSYL-L-HOMOCYSTEINE (3 entities in total)
• 機能のキーワード: methyltransferase, class i, sinefungin, s-adenosyl-l-homocysteine, complex, transferase
• 由来する生物種: Mycobacterium tuberculosis H37Rv
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 122240.64

構造登録者

Im, H.N.,Suh, S.W. (登録日: 2015-12-09, 公開日: 2016-06-29)

主引用文献

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

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: 26772148
DOI: 10.1016/j.jsb.2016.01.002

実験手法

X-RAY DIFFRACTION (2.9 Å)