The allosteric activator ATP induces a substrate-dependent alteration of the quaternary structure of a mutant aspartate transcarbamoylase impaired in active site closure

Protein Science

Volumn 5, Issue 11, 1996, Pages 2276-2286

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

^a BOSTON COLLEGE   (United States)

^b UNIVERSITÉ PARIS SACLAY   (France)

^c CNRS   (France)

^d BIOGEN   (United States)

Author keywords

domain closure; heterotropic regulation; homotropic cooperativity; protein structure function; site specific mutagenesis; solution X ray scattering

Indexed keywords

ADENOSINE TRIPHOSPHATE; ASPARTATE CARBAMOYLTRANSFERASE;

AMINO ACID ANALYSIS; AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; PRIORITY JOURNAL; PROTEIN QUATERNARY STRUCTURE; RADIATION SCATTERING; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS;

ESCHERICHIA COLI;

EID: 0029807135     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560051114     Document Type: Article

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