1lt8
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| , resolution 2.05Å | |||||||
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| Ligands: | , , | ||||||
| Activity: | Betaine--homocysteine S-methyltransferase, with EC number 2.1.1.5 | ||||||
| Related: | 1LT7
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Reduced Homo sapiens Betaine-Homocysteine S-Methyltransferase in Complex with S-(delta-carboxybutyl)-L-Homocysteine
OverviewOverview
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 StructureAbout this Structure
1LT8 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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
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