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1i42
From Proteopedia
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| - | [[Image:1i42.gif|left|200px]] | ||
| - | < | + | ==NMR STRUCTURE OF THE UBX DOMAIN FROM P47== |
| - | + | <StructureSection load='1i42' size='340' side='right'caption='[[1i42]]' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[1i42]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I42 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I42 FirstGlance]. <br> | |
| - | + | </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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1i42 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i42 OCA], [https://pdbe.org/1i42 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i42 RCSB], [https://www.ebi.ac.uk/pdbsum/1i42 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i42 ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | + | == Function == | |
| - | + | [https://www.uniprot.org/uniprot/NSF1C_RAT NSF1C_RAT] Reduces the ATPase activity of VCP. Necessary for the fragmentation of Golgi stacks during mitosis and for VCP-mediated reassembly of Golgi stacks after mitosis. May play a role in VCP-mediated formation of transitional endoplasmic reticulum (tER).<ref>PMID:9214505</ref> <ref>PMID:9824302</ref> <ref>PMID:10930451</ref> <ref>PMID:12411482</ref> | |
| - | + | == Evolutionary Conservation == | |
| - | + | [[Image:Consurf_key_small.gif|200px|right]] | |
| - | == | + | Check<jmol> |
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i4/1i42_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=1i42 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
p47 is the major protein identified in complex with the cytosolic AAA ATPase p97. It functions as an essential cofactor of p97-regulated membrane fusion, which has been suggested to disassemble t-t-SNARE complexes and prepare them for further rounds of membrane fusion. Here, we report the high-resolution NMR structure of the C-terminal domain from p47. It comprises a UBX domain and a 13 residue long structured N-terminal extension. The UBX domain adopts a characteristic ubiquitin fold with a betabetaalphabetabetaalphabeta secondary structure arrangement. Three hydrophobic residues from the N-terminal extension pack closely against a cleft in the UBX domain. We also identify, for the first time, the p97 interaction surface using NMR chemical shift perturbation studies. | p47 is the major protein identified in complex with the cytosolic AAA ATPase p97. It functions as an essential cofactor of p97-regulated membrane fusion, which has been suggested to disassemble t-t-SNARE complexes and prepare them for further rounds of membrane fusion. Here, we report the high-resolution NMR structure of the C-terminal domain from p47. It comprises a UBX domain and a 13 residue long structured N-terminal extension. The UBX domain adopts a characteristic ubiquitin fold with a betabetaalphabetabetaalphabeta secondary structure arrangement. Three hydrophobic residues from the N-terminal extension pack closely against a cleft in the UBX domain. We also identify, for the first time, the p97 interaction surface using NMR chemical shift perturbation studies. | ||
| - | + | Solution structure and interaction surface of the C-terminal domain from p47: a major p97-cofactor involved in SNARE disassembly.,Yuan X, Shaw A, Zhang X, Kondo H, Lally J, Freemont PS, Matthews S J Mol Biol. 2001 Aug 10;311(2):255-63. PMID:11478859<ref>PMID:11478859</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 1i42" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
| - | + | [[Category: Freemont PS]] | |
| - | [[Category: Freemont | + | [[Category: Kondo H]] |
| - | [[Category: Kondo | + | [[Category: Lally J]] |
| - | [[Category: Lally | + | [[Category: Matthews S]] |
| - | [[Category: Matthews | + | [[Category: Shaw A]] |
| - | [[Category: Shaw | + | [[Category: Yuan X]] |
| - | [[Category: Yuan | + | [[Category: Zhang X]] |
| - | [[Category: Zhang | + | |
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Current revision
NMR STRUCTURE OF THE UBX DOMAIN FROM P47
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Categories: Large Structures | Rattus norvegicus | Freemont PS | Kondo H | Lally J | Matthews S | Shaw A | Yuan X | Zhang X
