1vaz: Difference between revisions

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[[Image:1vaz.png|left|200px]]


{{STRUCTURE_1vaz| PDB=1vaz | SCENE= }}
==Solution structures of the p47 SEP domain==
<StructureSection load='1vaz' size='340' side='right'caption='[[1vaz]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1vaz]] 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=1VAZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VAZ 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=1vaz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vaz OCA], [https://pdbe.org/1vaz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vaz RCSB], [https://www.ebi.ac.uk/pdbsum/1vaz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vaz 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/va/1vaz_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=1vaz ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
p47 is a major adaptor molecule of the cytosolic AAA ATPase p97. The principal role of the p97-p47 complex is in regulation of membrane fusion events. Mono-ubiquitin recognition by p47 has also been shown to be crucial in the p97-p47-mediated Golgi membrane fusion events. Here, we describe the high-resolution solution structures of the N-terminal UBA domain and the central domain (SEP) from p47. The p47 UBA domain has the characteristic three-helix bundle fold and forms a highly stable complex with ubiquitin. We report the interaction surfaces of the two proteins and present a structure for the p47 UBA-ubiquitin complex. The p47 SEP domain adopts a novel fold with a betabetabetaalphaalphabeta secondary structure arrangement, where beta4 pairs in a parallel fashion to beta1. Based on biophysical studies, we demonstrate a clear propensity for the self-association of p47. Furthermore, p97 N binding abolishes p47 self-association, revealing the potential interaction surfaces for recognition of other domains within p97 or the substrate.


===Solution structures of the p47 SEP domain===
Structure, dynamics and interactions of p47, a major adaptor of the AAA ATPase, p97.,Yuan X, Simpson P, McKeown C, Kondo H, Uchiyama K, Wallis R, Dreveny I, Keetch C, Zhang X, Robinson C, Freemont P, Matthews S EMBO J. 2004 Apr 7;23(7):1463-73. Epub 2004 Mar 18. PMID:15029246<ref>PMID:15029246</ref>


{{ABSTRACT_PUBMED_15029246}}
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
==About this Structure==
<div class="pdbe-citations 1vaz" style="background-color:#fffaf0;"></div>
[[1vaz]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VAZ OCA].
== References ==
 
<references/>
==Reference==
__TOC__
<ref group="xtra">PMID:015029246</ref><references group="xtra"/>
</StructureSection>
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Dreveny, I.]]
[[Category: Dreveny I]]
[[Category: Freemont, P.]]
[[Category: Freemont P]]
[[Category: Keetch, C.]]
[[Category: Keetch C]]
[[Category: Kondo, H.]]
[[Category: Kondo H]]
[[Category: Matthews, S.]]
[[Category: Matthews S]]
[[Category: Mckeown, C.]]
[[Category: Mckeown C]]
[[Category: Robinson, C.]]
[[Category: Robinson C]]
[[Category: Simpson, P.]]
[[Category: Simpson P]]
[[Category: Uchiyama, K.]]
[[Category: Uchiyama K]]
[[Category: Wallis, R.]]
[[Category: Wallis R]]
[[Category: Yuan, X.]]
[[Category: Yuan X]]
[[Category: Zhang, X.]]
[[Category: Zhang X]]
[[Category: Beta-beta-beta-alpha-alpha-beta]]
[[Category: Lipid binding protein]]
[[Category: Novel fold]]

Latest revision as of 00:00, 28 December 2023

Solution structures of the p47 SEP domain

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