The structure of the proline utilization a proline dehydrogenase domain inactivated by N-propargylglycine provides insight into conformational changes induced by substrate binding and flavin reduction

Biochemistry

Volumn 49, Issue 3, 2010, Pages 560-569

  Srivastava, Dhiraj ^a   Zhu, Weidong ^c   Johnson Jr , William H ^d   Whitman, Christian P ^d   Becker, Donald F ^c   Tanner, John J ^a,b  

^a UNIVERSITY OF MISSOURI   (United States)

^b University of Missouri   (United States)

^c UNIVERSITY OF NEBRASKA LINCOLN   (United States)

^d UNIVERSITY OF TEXAS AT AUSTIN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; BINDING DOMAIN; CONFORMATIONAL CHANGE; CONSERVED RESIDUES; MEMBRANE AFFINITY; PROLINE DEHYDROGENASE; PROLINE UTILIZATION; RESOLUTION STRUCTURE; SUBSEQUENT REDUCTION; SUBSTRATE BINDING; TRANSCRIPTIONAL REPRESSORS;

BROADCASTING; ESCHERICHIA COLI;

MEMBRANE STRUCTURES;

ARGININE; ASPARTIC ACID; FLAVINE ADENINE NUCLEOTIDE; FLAVOPROTEIN; GLUTAMIC ACID; GLYCINE DERIVATIVE; LYSINE; N PROPARGYLGLYCINE; PROLINE; PROLINE DEHYDROGENASE; PROLINE UTILIZATION A; QUERCETIN; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; CONFORMATIONAL TRANSITION; COVALENT BOND; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME INACTIVATION; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN DOMAIN; PUT GENE; REDUCTION; REGULON; SIGNAL TRANSDUCTION;

ALKYNES; BINDING SITES; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; FLAVINS; GLYCINE; MODELS, MOLECULAR; OXIDATION-REDUCTION; PROLINE; PROLINE OXIDASE; PROTEIN CONFORMATION; SUBSTRATE SPECIFICITY;

ESCHERICHIA COLI;

EID: 74949118627     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi901717s     Document Type: Article

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