Crystal structure of CTP‐ligated T state aspartate transcarbamoylase at 2.5 Å resolution: Implications for ATCase mutants and the mechanism of negative cooperativity

Proteins: Structure, Function, and Bioinformatics

Volumn 15, Issue 2, 1993, Pages 147-176

  Kosman, Richard P ^a,b   Gouaux, J Eric ^c   Lipscomb, William N ^a  

^a HARVARD UNIVERSITY   (United States)

^b HARVARD MEDICAL SCHOOL   (United States)

^c MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

allosteric enzyme; alternative amino acid conformations; coordinate error; ligand induced negative cooperativity; pAR5 mutant; X ray crystallography

Indexed keywords

ASPARTATE CARBAMOYLTRANSFERASE; MUTANT PROTEIN;

ARTICLE; COMPUTER PROGRAM; CRYSTAL STRUCTURE; ENZYME CONFORMATION; ENZYME STRUCTURE; ENZYME SUBUNIT; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; STRUCTURE ACTIVITY RELATION; X RAY CRYSTALLOGRAPHY;

ALLOSTERIC SITE; AMINO ACID SEQUENCE; ASPARTATE CARBAMOYLTRANSFERASE; BINDING SITES; CYTIDINE TRIPHOSPHATE; ESCHERICHIA COLI; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; SUPPORT, NON-U.S. GOV'T; SUPPORT, U.S. GOV'T, P.H.S.; X-RAY DIFFRACTION;

RHIS;

EID: 0027399487     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.340150206     Document Type: Article

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