The first high pH structure of Escherichia coli aspartate transcarbamoylase

Proteins: Structure, Function and Bioinformatics

Volumn 74, Issue 2, 2009, Pages 318-327

  Stieglitz, Kimberly A ^a   Xia, Jiarong ^b   Kantrowitz, Evan R ^b  

^a UNIVERSITY OF MASSACHUSETTS BOSTON   (United States)

^b BOSTON COLLEGE   (United States)

Author keywords

Allosteric regulation; Aspartate transcarbamoylase; Bohr effect; Conformational change

Indexed keywords

ASPARTATE CARBAMOYLTRANSFERASE; BACTERIAL ENZYME; ESCHERICHIA COLI PROTEIN;

ALLOSTERISM; ARTICLE; BOHR EFFECT; CATALYSIS; CONFORMATIONAL TRANSITION; CRYSTALLIZATION; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME PURIFICATION; ENZYME STRUCTURE; ENZYME SUBSTRATE; ESCHERICHIA COLI; HYDROGEN BOND; MOLECULAR INTERACTION; MOLECULAR MODEL; NONHUMAN; PH; PKA; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN EXPRESSION; STRUCTURE ANALYSIS; THREE DIMENSIONAL IMAGING; X RAY DIFFRACTION; ANIMAL; CHEMISTRY; ENZYMOLOGY; METABOLISM; PROTEIN CONFORMATION; PROTEIN QUATERNARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; STRUCTURE ACTIVITY RELATION; X RAY CRYSTALLOGRAPHY;

ESCHERICHIA COLI;

ALLOSTERIC REGULATION; ANIMALS; ASPARTATE CARBAMOYLTRANSFERASE; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HYDROGEN-ION CONCENTRATION; PROTEIN CONFORMATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 59449093954     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22162     Document Type: Article

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