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Structure paper

TitleDisruption of Allosteric Response as an Unprecedented Mechanism of Resistance to Antibiotics.
Journal, issue, pagesJ. Am. Chem. Soc., Vol. 136, Page 9814-, Year 2014
Publish dateApr 30, 2013 (structure data deposition date)
AuthorsFishovitz, J. / Rojas-Altuve, A. / Otero, L.H. / Dawley, M. / Carrasco-Lopez, C. / Chang, M. / Hermoso, J.A. / Mobashery, S.
External linksJ. Am. Chem. Soc. / PubMed:24955778
MethodsX-ray diffraction
Resolution2.35 - 3 Å
Structure data

PDB-4bl2:
Crystal structure of PBP2a clinical mutant E150K from MRSA
Method: X-RAY DIFFRACTION / Resolution: 2.72 Å

PDB-4bl3:
Crystal structure of PBP2a clinical mutant N146K from MRSA
Method: X-RAY DIFFRACTION / Resolution: 3 Å

PDB-4cpk:
Crystal structure of PBP2a double clinical mutant N146K-E150K from MRSA
Method: X-RAY DIFFRACTION / Resolution: 2.35 Å

Chemicals

ChemComp-CD:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-MUR:
beta-muramic acid

Source
  • staphylococcus aureus (bacteria)
  • staphylococcus aureus (strain mu50 / atcc 700699) (bacteria)
KeywordsHYDROLASE / PENICILLIN BINDING PROTEINS / B-LACTUM ANTIBIOTICS / MRSA / ALLOSTERIC SITE / B-LACTAM ANTIBIOTICS / PENICILLIN-BINDING PROTEIN

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