1LT8

Reduced Homo sapiens Betaine-Homocysteine S-Methyltransferase in Complex with S-(delta-carboxybutyl)-L-Homocysteine

1LT8 の概要

• エントリーDOI: 10.2210/pdb1lt8/pdb
• 関連するPDBエントリー: 1LT7
• 分子名称: BETAINE-HOMOCYSTEINE METHYLTRANSFERASE, ZINC ION, S-(D-CARBOXYBUTYL)-L-HOMOCYSTEINE, ... (5 entities in total)
• 機能のキーワード: transferase, homocysteine metabolism, homocysteinemia, zinc, thiol alkyl transfer
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: Q93088
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 90673.71

構造登録者

Evans, J.C.,Huddler, D.P.,Jiracek, J.,Castro, C.,Millian, N.S.,Garrow, T.A.,Ludwig, M.L. (登録日: 2002-05-20, 公開日: 2002-09-11, 最終更新日: 2024-02-14)

主引用文献

Evans, J.C.,Huddler, D.P.,Jiracek, J.,Castro, C.,Millian, N.S.,Garrow, T.A.,Ludwig, M.L.
Betaine-homocysteine methyltransferase: zinc in a distorted barrel.
Structure, 10:1159-1171, 2002

PubMed Abstract: Betaine-homocysteine methyl transferase (BHMT) catalyzes the synthesis of methionine from betaine and homocysteine (Hcy), utilizing a zinc ion to activate Hcy. BHMT is a key liver enzyme that is important for homocysteine homeostasis. X-ray structures of human BHMT in its oxidized (Zn-free) and reduced (Zn-replete) forms, the latter in complex with the bisubstrate analog, S(delta-carboxybutyl)-L-homocysteine, were determined at resolutions of 2.15 A and 2.05 A. BHMT is a (beta/alpha)(8) barrel that is distorted to construct the substrate and metal binding sites. The zinc binding sequences G-V/L-N-C and G-G-C-C are at the C termini of strands beta6 and beta8. Oxidation to the Cys217-Cys299 disulfide and expulsion of Zn are accompanied by local rearrangements. The structures identify Hcy binding fingerprints and provide a prototype for the homocysteine S-methyltransferase family.

PubMed: 12220488
DOI: 10.1016/S0969-2126(02)00796-7

実験手法

X-RAY DIFFRACTION (2.05 Å)