Structural basis for ordered substrate binding and cooperativity in aspartate transcarbamoylase

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

Volumn 102, Issue 25, 2005, Pages 8881-8886

  Wang, Jie ^a   Stieglitz, Kimberly A ^a   Cardia, James P ^a   Kantrowitz, Evan R ^a  

^a BOSTON COLLEGE   (United States)

Author keywords

Allosteric transition; Homotropic cooperativity; Induced fit

Indexed keywords

ASPARTATE CARBAMOYLTRANSFERASE; ASPARTIC ACID; CARBAMOYL PHOSPHATE;

ALLOSTERISM; ARTICLE; BACTERIAL STRAIN; CATALYSIS; CONFORMATIONAL TRANSITION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME CONFORMATION; ENZYME ISOLATION; ENZYME PURIFICATION; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN QUATERNARY STRUCTURE; RADIATION SCATTERING; SIGNAL TRANSDUCTION; STRUCTURE ANALYSIS;

ALLOSTERIC REGULATION; AMINO ACID SEQUENCE; ASPARTATE CARBAMOYLTRANSFERASE; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; ELECTROSTATICS; ESCHERICHIA COLI; MODELS, MOLECULAR; PROTEIN CONFORMATION;

EID: 21144434991     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0503742102     Document Type: Article

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