1utx

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[[Image:1utx.jpg|left|200px]]
 
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{{Structure
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==Regulation of Cytolysin Expression by Enterococcus faecalis: Role of CylR2==
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|PDB= 1utx |SIZE=350|CAPTION= <scene name='initialview01'>1utx</scene>, resolution 1.90&Aring;
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<StructureSection load='1utx' size='340' side='right'caption='[[1utx]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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|SITE= <scene name='pdbsite=AC1:Na+Binding+Site+For+Chain+B'>AC1</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>
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<table><tr><td colspan='2'>[[1utx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UTX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UTX FirstGlance]. <br>
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|ACTIVITY=
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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]] 1.9&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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|DOMAIN=
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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=1utx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1utx OCA], [https://pdbe.org/1utx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1utx RCSB], [https://www.ebi.ac.uk/pdbsum/1utx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1utx ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1utx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1utx OCA], [http://www.ebi.ac.uk/pdbsum/1utx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1utx RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/Q8VL32_ENTFL Q8VL32_ENTFL]
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== Evolutionary Conservation ==
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'''REGULATION OF CYTOLYSIN EXPRESSION BY ENTEROCOCCUS FAECALIS: ROLE OF CYLR2'''
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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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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ut/1utx_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=1utx ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
Enterococcus faecalis is one of the major causes for hospital-acquired antibiotic-resistant infections. It produces an exotoxin, called cytolysin, which is lethal for a wide range of Gram-positive bacteria and is toxic to higher organisms. Recently, the regulation of the cytolysin operon was connected to autoinduction by a quorum-sensing mechanism involving the CylR1/CylR2 two-component regulatory system. We report here the crystal structure of CylR2 and its properties in solution as determined by heteronuclear NMR spectroscopy. The structure reveals a rigid dimer containing a helix-turn-helix DNA-binding motif as part of a five-helix bundle that is extended by an antiparallel beta-sheet. We show that CylR2 is a DNA-binding protein that binds specifically to a 22 bp fragment of the cytolysin promoter region. NMR chemical shift perturbation experiments identify surfaces involved in DNA binding and are in agreement with a model for the CylR2/DNA complex that attributes binding specificity to a complex network of CylR2/DNA interactions. Our results propose a mechanism where repression is achieved by CylR2 obstruction of the promoter preventing biosynthesis of the cytolysin operon transcript.
Enterococcus faecalis is one of the major causes for hospital-acquired antibiotic-resistant infections. It produces an exotoxin, called cytolysin, which is lethal for a wide range of Gram-positive bacteria and is toxic to higher organisms. Recently, the regulation of the cytolysin operon was connected to autoinduction by a quorum-sensing mechanism involving the CylR1/CylR2 two-component regulatory system. We report here the crystal structure of CylR2 and its properties in solution as determined by heteronuclear NMR spectroscopy. The structure reveals a rigid dimer containing a helix-turn-helix DNA-binding motif as part of a five-helix bundle that is extended by an antiparallel beta-sheet. We show that CylR2 is a DNA-binding protein that binds specifically to a 22 bp fragment of the cytolysin promoter region. NMR chemical shift perturbation experiments identify surfaces involved in DNA binding and are in agreement with a model for the CylR2/DNA complex that attributes binding specificity to a complex network of CylR2/DNA interactions. Our results propose a mechanism where repression is achieved by CylR2 obstruction of the promoter preventing biosynthesis of the cytolysin operon transcript.
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==About this Structure==
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Structure and DNA-binding properties of the cytolysin regulator CylR2 from Enterococcus faecalis.,Rumpel S, Razeto A, Pillar CM, Vijayan V, Taylor A, Giller K, Gilmore MS, Becker S, Zweckstetter M EMBO J. 2004 Sep 15;23(18):3632-42. Epub 2004 Sep 9. PMID:15359276<ref>PMID:15359276</ref>
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1UTX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UTX OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Structure and DNA-binding properties of the cytolysin regulator CylR2 from Enterococcus faecalis., Rumpel S, Razeto A, Pillar CM, Vijayan V, Taylor A, Giller K, Gilmore MS, Becker S, Zweckstetter M, EMBO J. 2004 Sep 15;23(18):3632-42. Epub 2004 Sep 9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15359276 15359276]
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</div>
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<div class="pdbe-citations 1utx" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Enterococcus faecalis]]
[[Category: Enterococcus faecalis]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Becker, S.]]
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[[Category: Becker S]]
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[[Category: Gilmore, M S.]]
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[[Category: Gilmore MS]]
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[[Category: Pillar, C M.]]
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[[Category: Pillar CM]]
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[[Category: Razeto, A.]]
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[[Category: Razeto A]]
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[[Category: Rumpel, S.]]
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[[Category: Rumpel S]]
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[[Category: Zweckstetter, M.]]
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[[Category: Zweckstetter M]]
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[[Category: dna-binding protein]]
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[[Category: helix-turn-helix]]
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[[Category: regulation of cytolysin operon]]
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[[Category: transcriptional repressor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:15:13 2008''
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Current revision

Regulation of Cytolysin Expression by Enterococcus faecalis: Role of CylR2

PDB ID 1utx

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