The allosteric activator Mg-ATP modifies the quaternary structure of the R-state of Escherichia coli aspartate transcarbamylase without altering the T ↔ R equilibrium

Journal of Molecular Biology

Volumn 309, Issue 3, 2001, Pages 817-832

  Fetler, L ^a,b   Vachette, P ^a,b  

^a CNRS   (France)

^b DIF   (France)

Author keywords

Allostery; ATCase; Conformational change; Enzyme regulation; Small angle X ray scattering

Indexed keywords

ADENOSINE TRIPHOSPHATE; ADENOSINE TRIPHOSPHATE MAGNESIUM; ASPARTATE CARBAMOYLTRANSFERASE; BACTERIAL ENZYME; MAGNESIUM; NUCLEOTIDE; PROTEIN SUBUNIT; SPARFOSIC ACID;

ALLOSTERISM; ARTICLE; BODY MOVEMENT; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME REGULATION; ESCHERICHIA COLI; METAL BINDING; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; PROTEIN QUATERNARY STRUCTURE;

ESCHERICHIA COLI;

EID: 0035827220     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2001.4681     Document Type: Article

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