240s Loop interactions stabilize the T state of Escherichia coli aspartate transcarbamoylase

Journal of Biological Chemistry

Volumn 279, Issue 22, 2004, Pages 23302-23310

  Alam, Neelima ^a   Stieglitz, Kimberly A ^a   Caban, Michael D ^a   Gourinath, Samudrala ^a,c   Tsuruta, Hiro ^b   Kantrowitz, Evan R ^a  

^a BOSTON COLLEGE   (United States)

^b SLAC NATIONAL ACCELERATOR LABORATORY   (United States)

^c JAWAHARLAL NEHRU UNIVERSITY   (India)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; CRYSTAL STRUCTURE; ENZYMES; STABILIZATION; X RAY SCATTERING;

LOOP RESIDUES; MUTANTS;

ESCHERICHIA COLI;

ALANINE; ASPARAGINE; ASPARTATE CARBAMOYLTRANSFERASE; LYSINE; SPARFOSIC ACID;

ANIMAL CELL; ARTICLE; CATALYSIS; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME STABILITY; ENZYME STRUCTURE; ESCHERICHIA COLI; METABOLIC REGULATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; PROTEIN QUATERNARY STRUCTURE; PROTEIN STABILITY; WILD TYPE; X RAY CRYSTALLOGRAPHY;

ASPARTATE CARBAMOYLTRANSFERASE; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; ENZYME STABILITY; ESCHERICHIA COLI; KINETICS; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; STRUCTURE-ACTIVITY RELATIONSHIP;

ANIMALIA; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA;

EID: 2542500802     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M401637200     Document Type: Article

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