Crystal complexes of a predicted S-adenosylmethionine-dependent methyltransferase reveal a typical AdoMet binding domain and a substrate recognition domain

Protein Science

Volumn 12, Issue 7, 2003, Pages 1432-1442

  Miller, Darcie J ^a   Ouellette, Nancy ^b   Evdokimova, Elena ^b   Savchenko, Alexei ^b   Edwards, Aled ^b   Anderson, Wayne F ^a  

^a NORTHWESTERN UNIVERSITY   (United States)

^b UNIVERSITY OF TORONTO   (Canada)

Author keywords

AdoHcy; AdoMet; Cell division; Methyltransferase; MraW; X ray crystal structure

Indexed keywords

METHYLTRANSFERASE; S ADENOSYLMETHIONINE;

ARTICLE; BACILLUS SUBTILIS; CELL DIVISION; CRYSTAL STRUCTURE; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; ESCHERICHIA COLI; GENOMICS; NONHUMAN; PHYLOGENY; PRIORITY JOURNAL; THERMOTOGA MARITIMA;

AMINO ACID SEQUENCE; BINDING SITES; CLONING, MOLECULAR; CONSERVED SEQUENCE; CRYSTALLOGRAPHY, X-RAY; METHYLTRANSFERASES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; S-ADENOSYLHOMOCYSTEINE; S-ADENOSYLMETHIONINE; SEQUENCE ALIGNMENT; SUBSTRATE SPECIFICITY; THERMOTOGA MARITIMA;

BACILLUS SUBTILIS; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; THERMOTOGA; THERMOTOGA MARITIMA;

EID: 0038309557     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.0302403     Document Type: Article

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