Structure of the E. coli aspartate transcarbamoylase trapped in the middle of the catalytic cycle

Journal of Molecular Biology

Volumn 352, Issue 2, 2005, Pages 478-486

  Stieglitz, Kimberly A ^a   Dusinberre, Kelly J ^a   Cardia, James P ^a   Tsuruta, Hiro ^b   Kantrowitz, Evan R ^a  

^a BOSTON COLLEGE   (United States)

^b SLAC NATIONAL ACCELERATOR LABORATORY   (United States)

Author keywords

Allosteric enzyme; Cooperativity; Enzyme mechanism; Small angle X ray scattering

Indexed keywords

ASPARTATE CARBAMOYLTRANSFERASE; BACTERIAL ENZYME;

ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME MECHANISM; ENZYME STRUCTURE; ENZYME SUBSTRATE; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; RADIATION SCATTERING; STRUCTURE ANALYSIS; X RAY CRYSTALLOGRAPHY;

ESCHERICHIA COLI;

EID: 23944462454     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.07.046     Document Type: Article

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