Allostery and substrate channeling in the tryptophan synthase bienzyme complex: Evidence for two subunit conformations and four quaternary states

Biochemistry

Volumn 52, Issue 37, 2013, Pages 6396-6411

  Niks, Dimitri ^a   Hilario, Eduardo ^a   Dierkers, Adam ^a   Ngo, Huu ^a,c   Borchardt, Dan ^b   Neubauer, Thomas J ^b   Fan, Li ^a   Mueller, Leonard J ^b   Dunn, Michael F ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c CALIFORNIA INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALLOSTERIC REGULATION; COMPUTATIONAL MODEL; CONFORMATIONAL STATE; LIGAND CONFORMATIONS; SUBSTRATE CHANNELINGS; SUBUNIT INTERFACES; TRYPTOPHAN SYNTHASE; X RAY CRYSTAL STRUCTURES;

AMINO ACIDS; CHEMICAL SHIFT; ENZYME ACTIVITY; LIGANDS; SUBSTRATES;

CONFORMATIONS;

INDOLE; MULTIENZYME COMPLEX; N (4' FLUOROMETHOXYBENZOYL) 2 AMINOETHYL PHOSPHATE; N (4' TRIFLUOROMETHOXYBENZENESULFONYL)) 2 AMINOETHYL PHOSPHATE; QUINONE DERIVATIVE; TRYPTOPHAN SYNTHASE; UNCLASSIFIED DRUG;

ALLOSTERISM; ARTICLE; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME SUBSTRATE COMPLEX; FLUORINE NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTON NUCLEAR MAGNETIC RESONANCE; X RAY CRYSTALLOGRAPHY;

ALLOSTERIC REGULATION; CRYSTALLOGRAPHY, X-RAY; INDOLES; LIGANDS; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN SUBUNITS; SALMONELLA TYPHIMURIUM; SERINE; TRYPTOPHAN SYNTHASE;

EID: 84884244026     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi400795e     Document Type: Article

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