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1lt7
From Proteopedia
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Oxidized Homo sapiens betaine-homocysteine S-methyltransferase in complex with four Sm(III) ions
Overview
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.
About this Structure
1LT7 is a Single protein structure of sequence from Homo sapiens with SM and CIT as ligands. Active as Betaine--homocysteine S-methyltransferase, with EC number 2.1.1.5 Full crystallographic information is available from OCA.
Reference
Betaine-homocysteine methyltransferase: zinc in a distorted barrel., Evans JC, Huddler DP, Jiracek J, Castro C, Millian NS, Garrow TA, Ludwig ML, Structure. 2002 Sep;10(9):1159-71. PMID:12220488
Page seeded by OCA on Mon Nov 12 18:04:01 2007
