1v92

From Proteopedia

(Difference between revisions)

Current revision

Solution structure of the UBA domain from p47, a major cofactor of the AAA ATPase p97

Structural highlights

1v92 is a 1 chain structure with sequence from Rattus norvegicus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).^[1] ^[2] ^[3] ^[4]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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.

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^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Kondo H, Rabouille C, Newman R, Levine TP, Pappin D, Freemont P, Warren G. p47 is a cofactor for p97-mediated membrane fusion. Nature. 1997 Jul 3;388(6637):75-8. PMID:9214505 doi:http://dx.doi.org/10.1038/40411
↑ Meyer HH, Kondo H, Warren G. The p47 co-factor regulates the ATPase activity of the membrane fusion protein, p97. FEBS Lett. 1998 Oct 23;437(3):255-7. PMID:9824302
↑ Roy L, Bergeron JJ, Lavoie C, Hendriks R, Gushue J, Fazel A, Pelletier A, Morre DJ, Subramaniam VN, Hong W, Paiement J. Role of p97 and syntaxin 5 in the assembly of transitional endoplasmic reticulum. Mol Biol Cell. 2000 Aug;11(8):2529-42. PMID:10930451
↑ Meyer HH, Wang Y, Warren G. Direct binding of ubiquitin conjugates by the mammalian p97 adaptor complexes, p47 and Ufd1-Npl4. EMBO J. 2002 Nov 1;21(21):5645-52. PMID:12411482
↑ Yuan X, Simpson P, McKeown C, Kondo H, Uchiyama K, Wallis R, Dreveny I, Keetch C, Zhang X, Robinson C, Freemont P, Matthews S. Structure, dynamics and interactions of p47, a major adaptor of the AAA ATPase, p97. EMBO J. 2004 Apr 7;23(7):1463-73. Epub 2004 Mar 18. PMID:15029246 doi:10.1038/sj.emboj.7600152

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1v92"

@@ Line 1: / Line 1: @@
-[[Image:1v92.gif|left|200px]]<br /><applet load="1v92" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1v92" />
-'''Solution structure of the UBA domain from p47, a major cofactor of the AAA ATPase p97'''<br />
-==Overview==
+==Solution structure of the UBA domain from p47, a major cofactor of the AAA ATPase p97==
-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.
+<StructureSection load='1v92' size='340' side='right'caption='[[1v92]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1v92]] 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=1V92 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V92 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=1v92 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v92 OCA], [https://pdbe.org/1v92 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v92 RCSB], [https://www.ebi.ac.uk/pdbsum/1v92 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v92 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/v9/1v92_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=1v92 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.
-==About this Structure==
+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>
-V92 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1V92 OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15029246 15029246]
+</div>
+<div class="pdbe-citations 1v92" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Rattus norvegicus]]
-[[Category: Single protein]]
+[[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: 3-helix bundle]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 04:31:02 2007''

1v92

From Proteopedia

Current revision

Solution structure of the UBA domain from p47, a major cofactor of the AAA ATPase p97

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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