3Q7Z: CBAP-acylated BlaR1 sensor domain from Staphylococcus aureus

The integral membrane protein BlaR1 of methicillin-resistant Staphylococcus aureus senses the presence of beta-lactam antibiotics in the milieu and transduces the information to the cytoplasm, where the biochemical events that unleash induction of antibiotic resistance mechanisms take place. We report herein by two-dimensional and three-dimensional NMR experiments of the sensor domain of BlaR1 in solution and by determination of an x-ray structure for the apo protein that Lys-392 of the antibiotic-binding site is posttranslationally modified by N(zeta)-carboxylation. Additional crystallographic and NMR data reveal that on acylation of Ser-389 by antibiotics, Lys-392 experiences N(zeta)-decarboxylation. This unique process, termed the lysine N(zeta)-decarboxylation switch, arrests the sensor domain in the activated ("on") state, necessary for signal transduction and all the subsequent biochemical processes. We present structural information on how this receptor activation process takes place, imparting longevity to the antibiotic-receptor complex that is needed for the induction of the antibiotic-resistant phenotype in methicillin-resistant S. aureus.
PDB ID: 3Q7ZDownload
MMDB ID: 91365
PDB Deposition Date: 2011/1/5
Updated in MMDB: 2017/11
Experimental Method:
x-ray diffraction
Resolution: 1.87  Å
Source Organism:
Similar Structures:
Biological Unit for 3Q7Z: monomeric; determined by author and by software (PISA)
Molecular Components in 3Q7Z
Label Count Molecule
Protein (1 molecule)
Beta-lactamase Regulatory Protein Blar1
Molecule annotation
Chemical (1 molecule)
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Citing MMDB