Why are the 2-oxoacid dehydrogenase complexes so large? Generation of an active trimeric complex

Biochemical Journal

Volumn 463, Issue 3, 2014, Pages 405-412

  Marrott, Nia L ^a   Marshall, Jacqueline J T ^b   Svergun, Dmitri I ^c   Crennell, Susan J ^a   Hough, David W ^a   Van Den Elsen, Jean M H ^a   Danson, Michael J ^a  

^a University of Bath   (United Kingdom)

^b IMPERIAL CANCER RESEARCH FUND   (United Kingdom)

^c EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

Author keywords

2 oxoacid dehydrogenase; Archaea; Macromolecular assembly; Multienzyme complex; Thermophile; X ray crystallography

Indexed keywords

2 OXOACID DEHYDROGENASE; DIHYDROLIPOAMIDE DEHYDROGENASE; E2 PROTEIN; MONOMER; MULTIENZYME COMPLEX; POLYPEPTIDE; UNCLASSIFIED DRUG; ARCHAEAL PROTEIN; OXIDOREDUCTASE;

ARTICLE; CARBOXY TERMINAL SEQUENCE; COMPLEX FORMATION; CRYSTAL STRUCTURE; DECARBOXYLATION; DENSITY GRADIENT CENTRIFUGATION; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME STABILITY; PROTEIN ASSEMBLY; PROTEIN EXPRESSION; PROTEIN STRUCTURE; STOP CODON; X RAY CRYSTALLOGRAPHY; CHEMISTRY; ENZYMOLOGY; GENETICS; HEAT; KINETICS; PROTEIN CONFORMATION; SMALL ANGLE SCATTERING; THERMOPLASMA;

ARCHAEAL PROTEINS; CRYSTALLOGRAPHY, X-RAY; DIHYDROLIPOAMIDE DEHYDROGENASE; ENZYME STABILITY; HOT TEMPERATURE; KINETICS; MULTIENZYME COMPLEXES; OXIDOREDUCTASES; PROTEIN CONFORMATION; SCATTERING, SMALL ANGLE; THERMOPLASMA;

EID: 84907834112     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20140359     Document Type: Article

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