Substrate-induced asymmetry and channel closure revealed by the apoenzyme structure of Mycobacterium tuberculosis phosphopantetheine adenylyltransferase

Protein Science

Volumn 13, Issue 9, 2004, Pages 2547-2552

  Morris, Van K ^a   Izard, Tina ^a  

^a ST JUDE CHILDREN S RESEARCH HOSPITAL   (United States)

Author keywords

Apoenzyme; Coenzyme A; Phosphopantetheine adenylyltransferase; Tuberculosis; X ray structure

Indexed keywords

ADENOSINE TRIPHOSPHATE; APOENZYME; BACTERIAL ENZYME; COENZYME A; DEPHOSPHOCOENZYME A; HEXAMER; OLIGOMER; PANTETHEINE PHOSPHATE; PANTETHEINE PHOSPHATE ADENYLYLTRANSFERASE; TRANSFERASE; UNCLASSIFIED DRUG;

ALLOSTERISM; ARTICLE; CATALYSIS; CHEMOREACTIVITY; CRYSTAL STRUCTURE; ENZYME INHIBITOR COMPLEX; ENZYME MECHANISM; ENZYME STRUCTURE; ENZYME SUBSTRATE; ENZYME SUBSTRATE COMPLEX; ENZYME SYNTHESIS; ESCHERICHIA COLI; LIGAND BINDING; MEMBRANE CHANNEL; MEMBRANE CHANNEL CLOSURE; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PRIORITY JOURNAL; X RAY CRYSTALLOGRAPHY;

APOENZYMES; BINDING SITES; COENZYME A; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI PROTEINS; LIGANDS; MODELS, MOLECULAR; MYCOBACTERIUM TUBERCULOSIS; NUCLEOTIDYLTRANSFERASES; PROTEIN CONFORMATION; STRUCTURAL HOMOLOGY, PROTEIN; SUBSTRATE SPECIFICITY;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; MYCOBACTERIUM; MYCOBACTERIUM TUBERCULOSIS; PROKARYOTA;

EID: 4344604153     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.04816904     Document Type: Article

References (20)

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