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==NMR STRUCTURE OF THE UBX DOMAIN FROM P47==
==NMR STRUCTURE OF THE UBX DOMAIN FROM P47==
<StructureSection load='1i42' size='340' side='right'caption='[[1i42]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
<StructureSection load='1i42' size='340' side='right'caption='[[1i42]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1i42]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. 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>
<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='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>
</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>
</table>
== Function ==
== 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>
[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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].
</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="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.
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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1i42" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Buffalo rat]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Freemont, P S]]
[[Category: Rattus norvegicus]]
[[Category: Kondo, H]]
[[Category: Freemont PS]]
[[Category: Lally, J]]
[[Category: Kondo H]]
[[Category: Matthews, S]]
[[Category: Lally J]]
[[Category: Shaw, A]]
[[Category: Matthews S]]
[[Category: Yuan, X]]
[[Category: Shaw A]]
[[Category: Zhang, X]]
[[Category: Yuan X]]
[[Category: Protein binding]]
[[Category: Zhang X]]
[[Category: Ubiquitin superfold]]
[[Category: Ubx]]
[[Category: Unusual n-terminal feature]]

Revision as of 07:44, 3 April 2024

NMR STRUCTURE OF THE UBX DOMAIN FROM P47

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