Direct observation in solution of a preexisting structural equilibrium for a mutant of the allosteric aspartate transcarbamoylase

Proceedings of the National Academy of Sciences of the United States of America

Volumn 104, Issue 2, 2007, Pages 495-500

  Fetler, Luc ^a,b   Kantrowitz, Evan R ^c   Vachette, Patrice ^d  

^a INSTITUT CURIE   (France)

^b CNRS   (France)

^c BOSTON COLLEGE   (United States)

^d INSTITUT D'OPTIQUE GRADUATE SCHOOL   (France)

Author keywords

Enzyme regulation; Homotropic cooperativity; Induced fit; Intersubunit interactions; Small angle x ray scattering

Indexed keywords

AMINE; ASPARTATE CARBAMOYLTRANSFERASE; ASPARTIC ACID; CARBAMOYL PHOSPHATE; LYSINE;

ALLOSTERISM; ARTICLE; BINDING AFFINITY; ENZYME STABILITY; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; LIGAND BINDING; METABOLISM; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN QUATERNARY STRUCTURE; SIGNAL TRANSDUCTION;

ALLOSTERIC REGULATION; ASPARTATE CARBAMOYLTRANSFERASE; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; PROTEIN STRUCTURE, QUATERNARY; RECOMBINANT PROTEINS; SCATTERING, RADIATION; SOLUTIONS; THERMODYNAMICS; X-RAYS;

ESCHERICHIA COLI;

EID: 33846298432     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0607641104     Document Type: Article

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