Insight into molybdenum cofactor deficiency provided by the crystal structure of the molybdenum cofactor biosynthesis protein MoaC

Structure

Volumn 8, Issue 7, 2000, Pages 709-718

  Wuebbens, Margot M ^a   Liu, Michael TW ^b   Rajagopalan, K V ^a   Schindelin, Hermann ^b  

^a DUKE UNIVERSITY MEDICAL CENTER   (United States)

^b STONY BROOK UNIVERSITY   (United States)

Author keywords

MoaC; Moco biosynthesis; Moco deficiency; Molybdenum cofactor (Moco); Protein crystallography

Indexed keywords

MOLYBDENUM; ARCHAEAL PROTEIN; BACTERIAL PROTEIN; ESCHERICHIA COLI PROTEIN; FERREDOXIN; HYBRID PROTEIN; METALLOPROTEIN; MOAC PROTEIN, E COLI; MOLYBDENUM COFACTOR; PTERIDINE DERIVATIVE; VEGETABLE PROTEIN;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; BIOSYNTHESIS; CARBON DIOXIDE FIXATION; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; HUMAN; PRIORITY JOURNAL; PROTEIN DEFICIENCY; PROTEIN EXPRESSION; PROTEIN STRUCTURE; AMINO ACID SEQUENCE; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; COENZYME; COMPARATIVE STUDY; ENZYMOLOGY; ESCHERICHIA COLI; GENE; GENETICS; ISOLATION AND PURIFICATION; METABOLISM; MOLECULAR EVOLUTION; MOLECULAR GENETICS; MULTIGENE FAMILY; PHYSIOLOGY; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS; SPECIES DIFFERENCE; STRUCTURE ACTIVITY RELATION; X RAY CRYSTALLOGRAPHY;

ARCHAEA; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; EUKARYOTA;

AMINO ACID SEQUENCE; ARCHAEAL PROTEINS; BACTERIAL PROTEINS; BINDING SITES; COENZYMES; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; EVOLUTION, MOLECULAR; FERREDOXINS; GENES; HUMANS; METALLOPROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MULTIGENE FAMILY; MUTAGENESIS, SITE-DIRECTED; PLANT PROTEINS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PTERIDINES; RECOMBINANT FUSION PROTEINS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SPECIES SPECIFICITY; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0034661492     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(00)00157-X     Document Type: Article

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