Solution structures of apo and holo biotinyl domains from acetyl coenzyme a carboxylase of Escherichia coli determined by triple-resonance nuclear magnetic resonance spectroscopy

Biochemistry

Volumn 38, Issue 16, 1999, Pages 5045-5053

  Roberts, Emma L ^a   Shu, Ningcheng ^a   Howard, Mark J ^a   Broadhurst, R William ^a   Chapman Smith, Anne ^b   Wallace, John C ^b   Morris, Tim ^c   Cronan Jr , John E ^c   Perham, Richard N ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^b UNIVERSITY OF ADELAIDE   (Australia)

^c UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACETYL COENZYME A CARBOXYLASE; APOENZYME; BIOTIN; BIOTINYL CARBOXY CARRIER PROTEIN; CARRIER PROTEIN; HYDROGEN; LYSINE; THREONINE; UNCLASSIFIED DRUG;

ARTICLE; BINDING SITE; BIOTINYLATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME CONFORMATION; ESCHERICHIA COLI; HYDROGEN BOND; MOLECULAR DYNAMICS; MOLECULAR MODEL; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN IMMOBILIZATION; STEREOCHEMISTRY; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS;

ACETYL-COA CARBOXYLASE; AMINO ACID SEQUENCE; APOENZYMES; BIOTIN; CARBON ISOTOPES; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; HOLOENZYMES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NITROGEN ISOTOPES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDE FRAGMENTS; PROTEIN STRUCTURE, SECONDARY; SOLUTIONS;

EID: 0033586767     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi982466o     Document Type: Article

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