Betaine-homocysteine methyltransferase: Zinc in a distorted barrel

John C. Evans, Donald P. Huddler, Jiri Jiracek, Carmen Castro, Norman S. Millian, Timothy A. Garrow, Martha L. Ludwig

Research output: Contribution to journalArticlepeer-review

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(δ-carboxybutyl)-L-homocysteine, were determined at resolutions of 2.15 Å and 2.05 Å. BHMT is a (β/α)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 β6 and β8. 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.

Original languageEnglish (US)
Pages (from-to)1159-1171
Number of pages13
JournalStructure
Volume10
Issue number9
DOIs
StatePublished - Sep 2002

Keywords

  • (β/α) barrel
  • Homocysteine
  • Methyltransfer
  • Signature sequences
  • Thiolate ligands
  • Zinc

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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