Structure of MMACHC reveals an arginine-rich pocket and a domain-swapped dimer for its B12 processing function

Biochemistry

Volumn 51, Issue 25, 2012, Pages 5083-5090

  Froese, D Sean ^a   Krojer, Tobias ^a   Wu, Xuchu ^b   Shrestha, Roshi ^a   Kiyani, Wasim ^a   Von Delft, Frank ^a   Gravel, Roy A ^b   Oppermann, Udo ^a   Yue, Wyatt W ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b UNIVERSITY OF CALGARY   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

AXIAL LIGAND; CATALYTIC FUNCTIONS; COFACTORS; DEALKYLATION; DIMERIC STRUCTURE; ENZYME COFACTORS; FLAVIN MONONUCLEOTIDES; GLUTATHIONES; NITROREDUCTASES; PROTEIN BINDS; SOLUTION STUDY; STRUCTURAL FRAMEWORKS;

CATALYSIS; DIMERS; ENZYMES; GENES; LIGANDS;

ARGININE;

COBALAMIN; DIMER; MUTANT PROTEIN; NITROREDUCTASE; PROTEIN; PROTEIN MMACHC; SCAFFOLD PROTEIN; UNCLASSIFIED DRUG; VITAMIN BINDING PROTEIN;

ARTICLE; CATALYSIS; DEALKYLATION; HUMAN; MISSENSE MUTATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN STRUCTURE;

ARGININE; CARRIER PROTEINS; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; HUMANS; MULTIENZYME COMPLEXES; MUTATION; PROTEIN MULTIMERIZATION; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN STRUCTURE, TERTIARY; VITAMIN B 12;

EID: 84862885395     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi300150y     Document Type: Article

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