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| | ==High-resolution structure determination of the CylR2 homodimer using intermonomer distances from paramagnetic relaxation enhancement and NMR dipolar couplings== | | ==High-resolution structure determination of the CylR2 homodimer using intermonomer distances from paramagnetic relaxation enhancement and NMR dipolar couplings== |
| - | <StructureSection load='2gzu' size='340' side='right' caption='[[2gzu]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''> | + | <StructureSection load='2gzu' size='340' side='right'caption='[[2gzu]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2gzu]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"enterococcus_proteiformis"_thiercelin_and_jouhaud_1903 "enterococcus proteiformis" thiercelin and jouhaud 1903]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GZU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GZU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2gzu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GZU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GZU FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1utx|1utx]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cylR2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1351 "Enterococcus proteiformis" Thiercelin and Jouhaud 1903])</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2gzu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gzu OCA], [https://pdbe.org/2gzu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gzu RCSB], [https://www.ebi.ac.uk/pdbsum/2gzu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gzu ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2gzu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gzu OCA], [http://pdbe.org/2gzu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2gzu RCSB], [http://www.ebi.ac.uk/pdbsum/2gzu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2gzu ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8VL32_ENTFL Q8VL32_ENTFL] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Enterococcus proteiformis thiercelin and jouhaud 1903]] | + | [[Category: Enterococcus faecalis]] |
| - | [[Category: Becker, S]] | + | [[Category: Large Structures]] |
| - | [[Category: Rumpel, S]] | + | [[Category: Becker S]] |
| - | [[Category: Zweckstetter, M]] | + | [[Category: Rumpel S]] |
| - | [[Category: Helix-loop-helix dna binding protein]] | + | [[Category: Zweckstetter M]] |
| - | [[Category: Transcription regulator]]
| + | |
| Structural highlights
Function
Q8VL32_ENTFL
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
Structure determination of homooligomeric proteins by NMR spectroscopy is difficult due to the lack of chemical shift perturbation data, which is very effective in restricting the binding interface in heterooligomeric systems, and the difficulty of obtaining a sufficient number of intermonomer distance restraints. Here we solved the high-resolution solution structure of the 15.4 kDa homodimer CylR2, the regulator of cytolysin production from Enterococcus faecalis, which deviates by 1.1 angstroms from the previously determined X-ray structure. We studied the influence of different experimental information such as long-range distances derived from paramagnetic relaxation enhancement, residual dipolar couplings, symmetry restraints and intermonomer Nuclear Overhauser Effect restraints on the accuracy of the derived structure. In addition, we show that it is useful to combine experimental information with methods of ab initio docking when the available experimental data are not sufficient to obtain convergence to the correct homodimeric structure. In particular, intermonomer distances may not be required when residual dipolar couplings are compared to values predicted on the basis of the charge distribution and the shape of ab initio docking solutions.
High-resolution structure determination of the CylR2 homodimer using paramagnetic relaxation enhancement and structure-based prediction of molecular alignment.,Rumpel S, Becker S, Zweckstetter M J Biomol NMR. 2008 Jan;40(1):1-13. Epub 2007 Nov 20. PMID:18026911[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Rumpel S, Becker S, Zweckstetter M. High-resolution structure determination of the CylR2 homodimer using paramagnetic relaxation enhancement and structure-based prediction of molecular alignment. J Biomol NMR. 2008 Jan;40(1):1-13. Epub 2007 Nov 20. PMID:18026911 doi:http://dx.doi.org/10.1007/s10858-007-9204-4
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