1nrf | pdb_00001nrf

C-terminal domain of the Bacillus licheniformis BlaR penicillin-receptor

spinqualitylabelsall models 1nrf, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1nrf is a 1 chain structure with sequence from "clostridium_licheniforme"_weigmann_1898 "clostridium licheniforme" weigmann 1898. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: blaR1 ("Clostridium licheniforme" Weigmann 1898) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [BLAR_BACLI] BlaR1 is a potential penicillin-binding protein required for induction of beta-lactamase in Bacillus licheniformis. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed As in several staphylococci, the synthesis of the Bacillus licheniformis 749/I beta-lactamase is an inducible phenomenon regulated by a signal-transducing membrane protein BlaR. The C-terminal domain of this multimodular protein is an extracellular domain which specifically recognizes beta-lactam antibiotics. When it binds a beta-lactam, a signal is transmitted by the transmembrane region to the intracellular loops. In response, the hydrolytic activity of the BlaR large cytoplasmic L3 loop is induced, and a cascade of reactions is generated, leading to the transcription of the beta-lactamase gene. Here, we describe the crystal structure of the extracellular penicillin-receptor domain of BlaR (residues 346-601) at 2.5 A resolution in order to understand why this domain, whose folding is very similar to that of class D beta-lactamases, behaves as a highly sensitive penicillin-binding protein rather than a beta-lactamase. Two residues of the BlaR C-terminal domain, Thr452 and Thr542, modify the hydrophobic characteristic of the class D beta-lactamase active site. Both residues seem to be in part responsible for the lack of beta-lactamase activity of the BlaR protein due to the stability of the acyl-enzyme. Although further experimental data are needed to fully understand the transmembrane induction process, the comparison of the BlaR sensor domain structure with those of class D beta-lactamase complexes and penicillin-binding proteins provides interesting elements to hypothesize on possible signal transmission mechanisms. Crystal structure of the sensor domain of the BlaR penicillin receptor from Bacillus licheniformis.,Kerff F, Charlier P, Colombo ML, Sauvage E, Brans A, Frere JM, Joris B, Fonze E Biochemistry. 2003 Nov 11;42(44):12835-43. PMID:14596597 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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