The chaperone FdsC for Rhodobacter capsulatus formate dehydrogenase binds the bis-molybdopterin guanine dinucleotide cofactor

FEBS Letters

Volumn 588, Issue 4, 2014, Pages 531-537

  Böhmer, Nadine ^a   Hartmann, Tobias ^a   Leimkühler, Silke ^a  

^a UNIVERSITY OF POTSDAM   (Germany)

Author keywords

bis MGD; Chaperone; Formate dehydrogenase; l cysteine desulfurase; Molybdenum cofactor

Indexed keywords

ALANINE; BACTERIAL PROTEIN; BIS MOLYBDOPTERIN GUANINE DINUCLEOTIDE COFACTOR; CHAPERONE; CYSTEINE; DINUCLEOTIDE; FORMATE DEHYDROGENASE; GUANINE DERIVATIVE; PROTEIN FDSC; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME BINDING; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; HETEROLOGOUS EXPRESSION; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DETERMINATION; PROTEIN EXPRESSION; PROTEIN PROTEIN INTERACTION; PROTEIN PURIFICATION; RHODOBACTER CAPSULATUS;

ESCHERICHIA COLI; RHODOBACTER CAPSULATUS;

BIS-MGD; CHAPERONE; FORMATE DEHYDROGENASE; L-CYSTEINE DESULFURASE; MOLYBDENUM COFACTOR;

COENZYMES; CONSERVED SEQUENCE; FORMATE DEHYDROGENASES; GUANINE NUCLEOTIDES; MOLECULAR CHAPERONES; OXIDOREDUCTASES, N-DEMETHYLATING; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; PTERINS; RHODOBACTER CAPSULATUS; SUBSTRATE SPECIFICITY;

EID: 84896725626     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2013.12.033     Document Type: Article

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