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| | <StructureSection load='2xi8' size='340' side='right'caption='[[2xi8]], [[Resolution|resolution]] 1.21Å' scene=''> | | <StructureSection load='2xi8' size='340' side='right'caption='[[2xi8]], [[Resolution|resolution]] 1.21Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2xi8]] 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 crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XI8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XI8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2xi8]] 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=2XI8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XI8 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.21Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2xj3|2xj3]], [[2xiu|2xiu]], [[1utx|1utx]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=2xi8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xi8 OCA], [http://pdbe.org/2xi8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xi8 RCSB], [http://www.ebi.ac.uk/pdbsum/2xi8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xi8 ProSAT]</span></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=2xi8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xi8 OCA], [https://pdbe.org/2xi8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xi8 RCSB], [https://www.ebi.ac.uk/pdbsum/2xi8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xi8 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8VL32_ENTFL Q8VL32_ENTFL] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Enterococcus proteiformis thiercelin and jouhaud 1903]] | + | [[Category: Enterococcus faecalis]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Becker, S]] | + | [[Category: Becker S]] |
| - | [[Category: Cho, M K]] | + | [[Category: Cho M-K]] |
| - | [[Category: Giller, K]] | + | [[Category: Giller K]] |
| - | [[Category: Grosse, C]] | + | [[Category: Grosse C]] |
| - | [[Category: Gruene, T]] | + | [[Category: Gruene T]] |
| - | [[Category: Karyagina, I]] | + | [[Category: Karyagina I]] |
| - | [[Category: Kim, H Y]] | + | [[Category: Kim H-Y]] |
| - | [[Category: Zweckstetter, M]] | + | [[Category: Zweckstetter M]] |
| - | [[Category: Hth dna-binding motif]]
| + | |
| - | [[Category: Transcription]]
| + | |
| Structural highlights
Function
Q8VL32_ENTFL
Publication Abstract from PubMed
Long-range structural information derived from paramagnetic relaxation enhancement observed in the presence of a paramagnetic nitroxide radical is highly useful for structural characterization of globular, modular and intrinsically disordered proteins, as well as protein-protein and protein-DNA complexes. Here we characterized the conformation of a spin-label attached to the homodimeric protein CylR2 using a combination of X-ray crystallography, electron paramagnetic resonance (EPR) and NMR spectroscopy. Close agreement was found between the conformation of the spin label observed in the crystal structure with interspin distances measured by EPR and signal broadening in NMR spectra, suggesting that the conformation seen in the crystal structure is also preferred in solution. In contrast, conformations of the spin label observed in crystal structures of T4 lysozyme are not in agreement with the paramagnetic relaxation enhancement observed for spin-labeled CylR2 in solution. Our data demonstrate that accurate positioning of the paramagnetic center is essential for high-resolution structure determination.
Integrated analysis of the conformation of a protein-linked spin label by crystallography, EPR and NMR spectroscopy.,Gruene T, Cho MK, Karyagina I, Kim HY, Grosse C, Giller K, Zweckstetter M, Becker S J Biomol NMR. 2011 Jan 28. PMID:21271275[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Gruene T, Cho MK, Karyagina I, Kim HY, Grosse C, Giller K, Zweckstetter M, Becker S. Integrated analysis of the conformation of a protein-linked spin label by crystallography, EPR and NMR spectroscopy. J Biomol NMR. 2011 Jan 28. PMID:21271275 doi:10.1007/s10858-011-9471-y
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