The Tipper-Strominger Hypothesis and Triggering of Allostery in Penicillin-Binding Protein 2a of Methicillin-Resistant Staphylococcus aureus (MRSA)

Journal of the American Chemical Society

Volumn 137, Issue 20, 2015, Pages 6500-6505

  Fishovitz, Jennifer ^a   Taghizadeh, Negin ^a   Fisher, Jed F ^a   Chang, Mayland ^a   Mobashery, Shahriar ^a  

^a UNIVERSITY OF NOTRE DAME   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; BINS; BIOSYNTHESIS; CELL MEMBRANES; CONFORMATIONS; ENZYME INHIBITION; PROTEINS;

CHEMICAL EQUATIONS; CONFORMATIONAL CHANGE; CONFORMATIONAL MOBILITY; ENVIRONMENTALLY SENSITIVE; FLUORESCENT PROBES; METHICILLIN-RESISTANT STAPHYLOCOCCUS AUREUS; MINIMAL INHIBITORY CONCENTRATION; PENICILLIN- BINDING PROTEINS;

ANTIBIOTICS;

BETA LACTAM ANTIBIOTIC; CEFEPIME; CEFTAROLINE; CEFTAZIDIME; GAMMA GLUTAMYLTRANSFERASE; IMIPENEM; MEROPENEM; OXACILLIN; PENICILLIN BINDING PROTEIN 2A; PIPERACILLIN; ANTIINFECTIVE AGENT; BETA LACTAM; PENICILLIN BINDING PROTEIN; PENICILLIN-BINDING PROTEIN 2A, STREPTOCOCCUS; PEPTIDE SYNTHASE;

ALLOSTERISM; ANTIBIOTIC RESISTANCE; ANTIBIOTIC SENSITIVITY; ARTICLE; CONFORMATIONAL TRANSITION; DRUG BINDING SITE; DRUG POTENTIATION; FLUORESCENCE IMAGING; METHICILLIN RESISTANT STAPHYLOCOCCUS AUREUS; MINIMUM INHIBITORY CONCENTRATION; MOLECULAR MIMICRY; NONHUMAN; ANTAGONISTS AND INHIBITORS; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; DRUG EFFECTS; METABOLISM; MOLECULAR MODEL;

ALLOSTERIC SITE; ANTI-BACTERIAL AGENTS; BETA-LACTAMS; METHICILLIN-RESISTANT STAPHYLOCOCCUS AUREUS; MODELS, MOLECULAR; MOLECULAR STRUCTURE; PENICILLIN-BINDING PROTEINS; PEPTIDE SYNTHASES;

EID: 84930202092     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/jacs.5b01374     Document Type: Article

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