1nrf

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(New page: 200px<br /><applet load="1nrf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nrf, resolution 2.50&Aring;" /> '''C-terminal domain of...)
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[[Image:1nrf.gif|left|200px]]<br /><applet load="1nrf" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1nrf, resolution 2.50&Aring;" />
 
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'''C-terminal domain of the Bacillus licheniformis BlaR penicillin-receptor'''<br />
 
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==Overview==
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==C-terminal domain of the Bacillus licheniformis BlaR penicillin-receptor==
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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.
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<StructureSection load='1nrf' size='340' side='right'caption='[[1nrf]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1nrf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis]. 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 [https://proteopedia.org/fgij/fg.htm?mol=1NRF FirstGlance]. <br>
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1NRF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NRF OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1nrf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nrf OCA], [https://pdbe.org/1nrf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nrf RCSB], [https://www.ebi.ac.uk/pdbsum/1nrf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nrf ProSAT]</span></td></tr>
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==Reference==
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</table>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14596597 14596597]
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== Function ==
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[https://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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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nr/1nrf_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1nrf ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Bacillus licheniformis]]
[[Category: Bacillus licheniformis]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Brans, A.]]
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[[Category: Brans A]]
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[[Category: Charlier, P.]]
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[[Category: Charlier P]]
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[[Category: Columbo, M.L.]]
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[[Category: Columbo ML]]
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[[Category: Fonze, E.]]
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[[Category: Fonze E]]
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[[Category: Frere, J.M.]]
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[[Category: Frere JM]]
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[[Category: Joris, B.]]
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[[Category: Joris B]]
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[[Category: Kerff, F.]]
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[[Category: Kerff F]]
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[[Category: Sauvage, E.]]
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[[Category: Sauvage E]]
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[[Category: bacillus licheniformis]]
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[[Category: beta-lactamase induction]]
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[[Category: penicillin-binding protein]]
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[[Category: penicillin-receptor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:30:21 2007''
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Current revision

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

PDB ID 1nrf

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