The β-lactamase gene regulator AmpR is a tetramer that recognizes and binds the D-Ala-D-Ala motif of its repressor UDP-N-acetylmuramic acid (MurNAc)-pentapeptide

Journal of Biological Chemistry

Volumn 290, Issue 5, 2015, Pages 2630-2643

  Vadlamani, Grishma ^a   Thomas, Misty D ^a,c   Patel, Trushar R ^a,d   Donald, Lynda J ^a   Reeve, Thomas M ^a   Stetefeld, Jörg ^a   Standing, Kenneth G ^a   Vocadlo, David J ^b   Mark, Brian L ^a  

^a UNIVERSITY OF MANITOBA   (Canada)

^b SIMON FRASER UNIVERSITY   (Canada)

^c NORTH CAROLINA A AND T STATE UNIVERSITY   (United States)

^d UNIVERSITY OF BIRMINGHAM   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

AMIDES; ANTIBIOTICS; BACTERIA; CONFORMATIONS; CRYSTAL STRUCTURE; DNA; MASS SPECTROMETRY; OLIGOMERS; PROTEINS; X RAY SCATTERING;

ANTIBIOTIC RESISTANCE; CITROBACTER FREUNDII; CONFORMATIONAL CHANGE; GRAM-NEGATIVE BACTERIA; INDUCIBLE EXPRESSION; N-ACETYLMURAMIC ACID; PSEUDOMONAS AERUGINOSA; TRANSCRIPTIONAL REGULATOR;

TRANSCRIPTION;

AMINO ACID; AMPR PROTEIN; DEXTRO ALANINE DEXTRO ALANINE; PENTAPEPTIDE; REGULATOR PROTEIN; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE N ACETYLMURAMIC ACID; ALANYLALANINE; AMPC BETA-LACTAMASES; AMPR PROTEIN, BACTERIA; BACTERIAL PROTEIN; BETA LACTAMASE; DIPEPTIDE; PEPTIDOGLYCAN; PROTEIN BINDING; UDP-N-ACETYLMURAMIC ACID PENTAPEPTIDE;

AMPR GENE; ARTICLE; BINDING SITE; CITROBACTER FREUNDII; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; DNA PROTEIN COMPLEX; MASS SPECTROMETRY; METABOLITE; MOLECULAR RECOGNITION; OPERON; PREDICTION; PROMOTER REGION; PROTEIN DNA BINDING; PROTEIN REFOLDING; REGULATOR GENE; X RAY CRYSTALLOGRAPHY; ANALOGS AND DERIVATIVES; CHEMISTRY; METABOLISM; SMALL ANGLE SCATTERING;

CITROBACTER FREUNDII; ENTEROBACTERIACEAE; NEGIBACTERIA; PSEUDOMONAS AERUGINOSA;

BACTERIAL PROTEINS; BETA-LACTAMASES; DIPEPTIDES; PEPTIDOGLYCAN; PROTEIN BINDING; SCATTERING, SMALL ANGLE; URIDINE DIPHOSPHATE N-ACETYLMURAMIC ACID;

EID: 84921883395     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.618199     Document Type: Article

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