2xiu
From Proteopedia
(Difference between revisions)
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| - | + | ==HIGH RESOLUTION STRUCTURE OF MTSL-TAGGED CYLR2.== | |
| - | + | <StructureSection load='2xiu' size='340' side='right' caption='[[2xiu]], [[Resolution|resolution]] 1.50Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[2xiu]] is a 2 chain structure with 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=2XIU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XIU 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>, <scene name='pdbligand=MTN:S-[(1-OXYL-2,2,5,5-TETRAMETHYL-2,5-DIHYDRO-1H-PYRROL-3-YL)METHYL]+METHANESULFONOTHIOATE'>MTN</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2xi8|2xi8]], [[1utx|1utx]]</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=2xiu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xiu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xiu RCSB], [http://www.ebi.ac.uk/pdbsum/2xiu PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:21271275</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Enterococcus faecalis]] | [[Category: Enterococcus faecalis]] | ||
| - | [[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: Dna binding protein]] | [[Category: Dna binding protein]] | ||
[[Category: Hth-dna binding motif]] | [[Category: Hth-dna binding motif]] | ||
Revision as of 12:42, 18 December 2014
HIGH RESOLUTION STRUCTURE OF MTSL-TAGGED CYLR2.
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