1nrf

<table><tr><td colspan='2'>[[1nrf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"clostridium_licheniforme"_weigmann_1898 "clostridium licheniforme" weigmann 1898]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NRF OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1NRF FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">blaR1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1402 "Clostridium licheniforme" Weigmann 1898])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1nrf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nrf OCA], [http://pdbe.org/1nrf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1nrf RCSB], [http://www.ebi.ac.uk/pdbsum/1nrf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1nrf ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/BLAR_BACLI BLAR_BACLI]] BlaR1 is a potential penicillin-binding protein required for induction of beta-lactamase in Bacillus licheniformis.

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== 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<ref>PMID:14596597</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1nrf" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Clostridium licheniforme weigmann 1898]]

[[Category: Brans, A]]

[[Category: Charlier, P]]

[[Category: Columbo, M L]]

[[Category: Fonze, E]]

[[Category: Frere, J M]]

[[Category: Joris, B]]

[[Category: Kerff, F]]

[[Category: Sauvage, E]]

[[Category: Penicillin-receptor]]