A single amino acid substitution in the active site of Escherichia coli aspartate transcarbamoylase prevents the allosteric transition

Journal of Molecular Biology

Volumn 349, Issue 2, 2005, Pages 413-423

  Stieglitz, Kimberly A ^a   Pastra Landis, Styliani C ^b   Xia, Jiarong ^a   Tsuruta, Hiro ^c   Kantrowitz, Evan R ^a   Huber, R ^d  

^a BOSTON COLLEGE   (United States)

^b WHEATON COLLEGE   (United States)

^c SLAC NATIONAL ACCELERATOR LABORATORY   (United States)

^d NONE

Author keywords

Allosteric enzyme; Electrostatics; Poisson Boltzmann equation; Polar contacts; Small angle X ray scattering

Indexed keywords

ALANINE; AMINO ACID; ARGININE; ASPARTATE CARBAMOYLTRANSFERASE; ASPARTIC ACID; CARBAMOYL PHOSPHATE; CARBAMOYLTRANSFERASE; GLUTAMINE; HISTAMINE;

ALLOSTERISM; AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; BINDING SITE; CONTROLLED STUDY; ELECTRICITY; ESCHERICHIA COLI; KINETICS; LIGHT SCATTERING; MUTANT; NONHUMAN; PRIORITY JOURNAL; PROTEIN STRUCTURE; RADIATION SCATTERING; WILD TYPE; X RAY CRYSTALLOGRAPHY;

ESCHERICHIA COLI;

EID: 18844437767     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.03.073     Document Type: Article

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