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1v92

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Revision as of 06:28, 6 October 2021

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 Buffalo rat. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
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 3: / Line 3: @@
 <StructureSection load='1v92' size='340' side='right'caption='[[1v92]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1v92]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1V92 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1v92]] 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=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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1v92 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v92 OCA], [http://pdbe.org/1v92 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1v92 RCSB], [http://www.ebi.ac.uk/pdbsum/1v92 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1v92 ProSAT]</span></td></tr>
+</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 ==
-[[http://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 ==
 [[Image:Consurf_key_small.gif|200px|right]]

1v92

From Proteopedia

Revision as of 06:28, 6 October 2021

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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