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Structure paper

TitleUnbound and Acylated Structures of the Mecr1 Extracellular Antibiotic-Sensor Domain Provide Insights Into the Signal-Transduction System that Triggers Methicillin Resistance.
Journal, issue, pagesJ. Mol. Biol., Vol. 361, Page 506-, Year 2006
Publish dateJun 27, 2006 (structure data deposition date)
AuthorsMarrero, A. / Mallorqui-Fernandez, G. / Guevara, T. / Garcia-Castellanos, R. / Gomis-Ruth, F.X.
External linksJ. Mol. Biol. / PubMed:16846613
MethodsX-ray diffraction
Resolution1.8 - 2.4 Å
Structure data

PDB-2iwb:
MecR1 unbound extracellular antibiotic-sensor domain.
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-2iwc:
Benzylpenicilloyl-acylated MecR1 extracellular antibiotic-sensor domain.
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-2iwd:
Oxacilloyl-acylated MecR1 extracellular antibiotic-sensor domain.
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

Chemicals

ChemComp-NI:
NICKEL (II) ION

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-PNM:
OPEN FORM - PENICILLIN G / antibiotic*YM

ChemComp-1S6:
(2R,4S)-5,5-dimethyl-2-[(1R)-1-{[(5-methyl-3-phenyl-1,2-oxazol-4-yl)carbonyl]amino}-2-oxoethyl]-1,3-thiazolidine-4-carb / antibiotic*YM

Source
  • staphylococcus aureus (bacteria)
  • synthetic construct (others)
  • staphylococcus aureus subsp. aureus n315 (bacteria)
KeywordsANTIBIOTIC RESISTANCE / BACTERIAL ANTIBIOTIC RESISTANCE / METHICILLIN RESISTANCE / BETA-LACTAMIC ANTIBIOTICS / MRSA / BETA-LACTAMASE / PENICILLIN-BINDING PROTEIN / BENZYLPENICILLIN / OXACILLIN

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