Crystal structure of rat liver betaine homocysteine S-methyltransferase reveals new oligomerization features and conformational changes upon substrate binding

Journal of Molecular Biology

Volumn 338, Issue 4, 2004, Pages 771-782

  González, Beatriz ^a   Pajares, María A ^b   Martínez Ripoll, Martín ^a   Blundell, Tom L ^c   Sanz Aparicio, Julia ^a  

^a INSTITUTO DE QUÍMICA FÍSICA ROCASOLANO   (Spain)

^b INSTITUTO DE INVESTIGACIONES BIOMÉDICAS ALBERTO SOLS   (Spain)

^c UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

Betaine homocysteine S methyltransferase; BHMT, betaine homocysteine S methyltransferase from rat liver; h BHMT, human betaine homocysteine S methyltransferase; Hcy, homocysteine; Subunit interactions; X ray structure; Zn ligands; Zn metalloenzyme

Indexed keywords

BETAINE HOMOCYSTEINE METHYLTRANSFERASE; HOMOCYSTEINE; LIVER ENZYME; UNCLASSIFIED DRUG;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CONFORMATION; CRYSTAL STRUCTURE; ENZYME STRUCTURE; ENZYME SUBSTRATE; ENZYME SUBSTRATE COMPLEX; ENZYME SUBUNIT; HYDROPHOBICITY; MOLECULAR INTERACTION; MOLECULAR RECOGNITION; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; RAT; SITE DIRECTED MUTAGENESIS;

EID: 1942457281     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.03.005     Document Type: Article

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