Direct evidence for the size and conformational variability of the pyruvate dehydrogenase complex revealed by three-dimensional electron microscopy. The "breathing" core and its functional relationship to protein dynamics

Journal of Biological Chemistry

Volumn 276, Issue 24, 2001, Pages 21704-21713

  Zhou, Z Hong ^a   Liao, Wangcai ^a   Cheng, R Holland ^b   Lawson, J E ^c,d   McCarthy, D B ^c,e   Reed, Lester J ^c   Stoops, James K ^a  

^a UNIVERSITY OF TEXAS MEDICAL SCHOOL   (United States)

^b KAROLINSKA INSTITUTE   (Sweden)

^c UNIVERSITY OF TEXAS AT AUSTIN   (United States)

^d Premier Research   (United States)

^e CIPHERGEN BIOSYSTEMS INC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ELECTRON MICROSCOPY; MOLECULES; MORPHOLOGY; YEAST;

TRIMERS;

ENZYMES;

BACTERIAL ENZYME; CORE PROTEIN; DIHYDROLIPOAMIDE ACETYLTRANSFERASE; FUNGAL ENZYME; OLIGOMER; PROTEIN; PYRUVATE DEHYDROGENASE COMPLEX; ACYLTRANSFERASE; PDA2 PROTEIN, S CEREVISIAE; PROTEIN SUBUNIT; SACCHAROMYCES CEREVISIAE PROTEIN;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CRYSTAL STRUCTURE; ELECTRON MICROSCOPY; ENZYME CONFORMATION; ENZYME STRUCTURE; ENZYME SUBUNIT; GEOBACILLUS STEAROTHERMOPHILUS; MOLECULAR DYNAMICS; MOLECULAR SIZE; NONHUMAN; PHYLOGENY; PRIORITY JOURNAL; PROTEIN DYNAMICS; PROTEIN FUNCTION; SACCHAROMYCES CEREVISIAE; TEMPERATURE; THREE DIMENSIONAL IMAGING; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYMOLOGY; IMAGE PROCESSING; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; ULTRASTRUCTURE;

BACTERIA (MICROORGANISMS); GEOBACILLUS STEAROTHERMOPHILUS; ILEX COOKII; SACCHAROMYCES; SACCHAROMYCES CEREVISIAE;

ACETYLTRANSFERASES; BACILLUS STEAROTHERMOPHILUS; BINDING SITES; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE; IMAGE PROCESSING, COMPUTER-ASSISTED; MICROSCOPY, ELECTRON; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN SUBUNITS; PYRUVATE DEHYDROGENASE COMPLEX; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS;

EID: 0035877764     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M101765200     Document Type: Article

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