Crystal structure and solution characterization of the activation domain of human methionine synthase

FEBS Journal

Volumn 274, Issue 3, 2007, Pages 738-750

  Wolthers, Kirsten R ^a   Toogood, Helen S ^a   Jowitt, Thomas A ^a   Marshall, Ker R ^b   Leys, David ^a   Scrutton, Nigel S ^a  

^a UNIVERSITY OF MANCHESTER   (United Kingdom)

^b UNIVERSITY OF LEICESTER   (United Kingdom)

Author keywords

Activation domain; Cobalamin dependent enzyme; Methionine synthase; Methionine synthase reductase; S adenosyl methionine

Indexed keywords

COBALAMIN; FLAVINE MONONUCLEOTIDE; METHIONINE SYNTHASE; S ADENOSYLMETHIONINE;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CRYSTAL STRUCTURE; DIMERIZATION; ELECTRON TRANSPORT; ENZYME ACTIVATION; ENZYME ANALYSIS; ENZYME BINDING; ENZYME REACTIVATION; ENZYME STRUCTURE; ESCHERICHIA COLI; FLUORESCENCE; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN INTERACTION; SEQUENCE HOMOLOGY;

5-METHYLTETRAHYDROFOLATE-HOMOCYSTEINE S-METHYLTRANSFERASE; AMINO ACID MOTIFS; AMINO ACID SEQUENCE; BINDING SITES; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; FERREDOXIN-NADP REDUCTASE; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; POLYMERASE CHAIN REACTION; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; S-ADENOSYLMETHIONINE; SEQUENCE ALIGNMENT; VITAMIN B 12;

ESCHERICHIA COLI;

EID: 33846441222     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2006.05618.x     Document Type: Article

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