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2ru6
From Proteopedia
(Difference between revisions)
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| - | + | ==The pure alternative state of ubiquitin== | |
| - | === | + | <StructureSection load='2ru6' size='340' side='right' caption='[[2ru6]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[2ru6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RU6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RU6 FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2rsu|2rsu]]</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">UBC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ru6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ru6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ru6 RCSB], [http://www.ebi.ac.uk/pdbsum/2ru6 PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | We present the nuclear Overhauser effect-based structure determination of the Q41N variant of ubiquitin at 2500 bar, where the alternatively folded N2 state is 97% populated. This allows us to characterize the structure of the "pure" N2 state of ubiquitin. The N2 state shows a substantial change in the orientation of strand beta5 compared to that of the normal folded N1 state, which matches the changes seen upon binding of ubiquitin to ubiquitin-activating enzyme E1. The recognition of E1 by ubiquitin is therefore best explained by conformational selection rather than induced-fit motion. | ||
| - | + | Close Identity between Alternatively Folded State N2 of Ubiquitin and the Conformation of the Protein Bound to the Ubiquitin-Activating Enzyme.,Kitazawa S, Kameda T, Kumo A, Yagi-Utsumi M, Baxter NJ, Kato K, Williamson MP, Kitahara R Biochemistry. 2014 Jan 28;53(3):447-9. doi: 10.1021/bi401617n. Epub 2014 Jan 10. PMID:24401037<ref>PMID:24401037</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | == | + | <references/> |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
| + | [[Category: Human]] | ||
[[Category: Baxter, N.]] | [[Category: Baxter, N.]] | ||
[[Category: Kameda, T.]] | [[Category: Kameda, T.]] | ||
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[[Category: High-pressure nmr]] | [[Category: High-pressure nmr]] | ||
[[Category: Protein binding]] | [[Category: Protein binding]] | ||
| + | [[Category: Q41n variant]] | ||
[[Category: Ubiquitin]] | [[Category: Ubiquitin]] | ||
Revision as of 12:54, 18 May 2014
The pure alternative state of ubiquitin
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