1IM8

Crystal structure of YecO from Haemophilus influenzae (HI0319), a methyltransferase with a bound S-adenosylhomocysteine

1IM8 の概要

• エントリーDOI: 10.2210/pdb1im8/pdb
• 分子名称: YecO, CHLORIDE ION, S-ADENOSYL-L-HOMOSELENOCYSTEINE, ... (4 entities in total)
• 機能のキーワード: methyltransferase, adenosylhomocysteine, structural genomics, hypothetical protein, structure 2 function project, s2f, transferase
• 由来する生物種: Haemophilus influenzae Rd
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 56963.66

構造登録者

Lim, K.,Zhang, H.,Tempczyk, A.,Bonander, N.,Toedt, J.,Howard, A.,Eisenstein, E.,Herzberg, O.,Structure 2 Function Project (S2F) (登録日: 2001-05-10, 公開日: 2001-11-07, 最終更新日: 2024-11-20)

主引用文献

Lim, K.,Zhang, H.,Tempczyk, A.,Bonander, N.,Toedt, J.,Howard, A.,Eisenstein, E.,Herzberg, O.
Crystal structure of YecO from Haemophilus influenzae (HI0319) reveals a methyltransferase fold and a bound S-adenosylhomocysteine.
Proteins, 45:397-407, 2001

PubMed Abstract: The crystal structure of YecO from Haemophilus influenzae (HI0319), a protein annotated in the sequence databases as hypothetical, and that has not been assigned a function, has been determined at 2.2-A resolution. The structure reveals a fold typical of S-adenosyl-L-methionine-dependent (AdoMet) methyltransferase enzymes. Moreover, a processed cofactor, S-adenosyl-L-homocysteine (AdoHcy), is bound to the enzyme, further confirming the biochemical function of HI0319 and its sequence family members. An active site arginine, shielded from bulk solvent, interacts with an anion, possibly a chloride ion, which in turn interacts with the sulfur atom of AdoHcy. The AdoHcy and nearby protein residues delineate a small solvent-excluded substrate binding cavity of 162 A(3) in volume. The environment surrounding the cavity indicates that the substrate molecule contains a hydrophobic moiety and an anionic group. Many of the residues that define the cavity are invariant in the HI0319 sequence family but are not conserved in other methyltransferases. Therefore, the substrate specificity of YecO enzymes is unique and differs from the substrate specificity of all other methyltransferases sequenced to date. Examination of the Enzyme Commission list of methyltransferases prompted a manual inspection of 10 possible substrates using computer graphics and suggested that the ortho-substituted benzoic acids fit best in the active site.

PubMed: 11746687
DOI: 10.1002/prot.10004

実験手法

X-RAY DIFFRACTION (2.2 Å)