NMR-based structural analysis of threonylcarbamoyl-AMP synthase and its substrate interactions

Journal of Biological Chemistry

Volumn 290, Issue 33, 2015, Pages 20032-20043

  Harris, Kimberly A ^a,b   Bobay, Benjamin G ^a   Sarachan, Kathryn L ^b   Sims, Alexis F ^b   Bilbille, Yann ^a   Deutsch, Christopher ^c   Iwata Reuyl, Dirk ^c   Agris, Paul F ^b  

^a NORTH CAROLINA STATE UNIVERSITY   (United States)

^b STATE UNIVERSITY OF NEW YORK   (United States)

^c PORTLAND STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BINDING SITES; BIOCHEMISTRY; BIOSYNTHESIS; ESCHERICHIA COLI; SUBSTRATES;

BIOSYNTHETIC PATHWAY; CONFORMATIONAL FLEXIBILITY; ENZYMATIC MECHANISMS; ENZYMATIC REACTION; HYDROPHOBIC BINDING; POST-TRANSCRIPTIONAL MODIFICATION; SOLUTION STRUCTURES; SUBSTRATE INTERACTION;

PROTEINS;

ADENINE; ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEIN; SYNTHETASE; THREONINE; TSAC PROTEIN; UNCLASSIFIED DRUG; ADENOSINE PHOSPHATE; LIGASE;

ARTICLE; BINDING SITE; ENZYME ANALYSIS; ENZYME CONFORMATION; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; ENZYME SYNTHESIS; ESCHERICHIA COLI; HYDROPHOBICITY; ISOTHERMAL TITRATION CALORIMETRY; MOLECULAR DOCKING; MOLECULAR MODEL; MOLECULAR RECOGNITION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME SPECIFICITY; METABOLISM; PROTEIN CONFORMATION;

ESCHERICHIA COLI;

ADENOSINE MONOPHOSPHATE; LIGASES; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; SUBSTRATE SPECIFICITY; THREONINE;

EID: 84939645471     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.631242     Document Type: Article

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