2x5n

From Proteopedia

(Difference between revisions)

Current revision

Crystal Structure of the SpRpn10 VWA domain

Structural highlights

2x5n is a 1 chain structure with sequence from Schizosaccharomyces pombe. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.3Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RPN10_SCHPO Protects ubiquitin chains against dissambly by deubiquitinating enzymes thereby promoting protein degradation.^[1] ^[2]

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

Schizosaccharomyces pombe Rpn10 (SpRpn10) is a proteasomal ubiquitin (Ub) receptor located within the 19S regulatory particle where it binds to subunits of both the base and lid sub-particles. We have solved the structure of full-length SpRpn10 by determining the crystal structure of the VWA domain and characterising the full-length protein by NMR. We demonstrate that the single Ub interacting motif (UIM) of SpRpn10 forms a 1:1 complex with K48-linked diUb, which it binds selectively over monoUb and K63-linked diUb. We further show that the SpRpn10 UIM binds to SpRpn12, a subunit of the lid sub-particle, with an affinity comparable to Lys48-linked diUb. This is the first observation of a UIM binding other than a Ub fold and suggests that SpRpn12 could modulate the activity of SpRpn10 as a proteasomal Ub receptor.

The structure of RPN10 and its interactions with polyubiquitin chains and the proteasome subunit RPN12.,Riedinger C, Boehringer J, Trempe JF, Lowe ED, Brown NR, Gehring K, Noble ME, Gordon C, Endicott JA J Biol Chem. 2010 Aug 24. PMID:20739285^[3]

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

References

↑ Wilkinson CR, Ferrell K, Penney M, Wallace M, Dubiel W, Gordon C. Analysis of a gene encoding Rpn10 of the fission yeast proteasome reveals that the polyubiquitin-binding site of this subunit is essential when Rpn12/Mts3 activity is compromised. J Biol Chem. 2000 May 19;275(20):15182-92. PMID:10809753
↑ Hartmann-Petersen R, Hendil KB, Gordon C. Ubiquitin binding proteins protect ubiquitin conjugates from disassembly. FEBS Lett. 2003 Jan 30;535(1-3):77-81. PMID:12560082
↑ Riedinger C, Boehringer J, Trempe JF, Lowe ED, Brown NR, Gehring K, Noble ME, Gordon C, Endicott JA. The structure of RPN10 and its interactions with polyubiquitin chains and the proteasome subunit RPN12. J Biol Chem. 2010 Aug 24. PMID:20739285 doi:10.1074/jbc.M110.134510

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2x5n"

@@ Line 3: / Line 3: @@
 <StructureSection load='2x5n' size='340' side='right'caption='[[2x5n]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2x5n]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cbs_356 Cbs 356]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X5N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X5N FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2x5n]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X5N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X5N FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=2x5n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x5n OCA], [https://pdbe.org/2x5n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x5n RCSB], [https://www.ebi.ac.uk/pdbsum/2x5n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x5n ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/RPN10_SCHPO RPN10_SCHPO]] Protects ubiquitin chains against dissambly by deubiquitinating enzymes thereby promoting protein degradation.<ref>PMID:10809753</ref> <ref>PMID:12560082</ref>
+[https://www.uniprot.org/uniprot/RPN10_SCHPO RPN10_SCHPO] Protects ubiquitin chains against dissambly by deubiquitinating enzymes thereby promoting protein degradation.<ref>PMID:10809753</ref> <ref>PMID:12560082</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 35: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Cbs 356]]
 [[Category: Large Structures]]
-[[Category: Boehringer, J]]
+[[Category: Schizosaccharomyces pombe]]
-[[Category: Brown, N R]]
+[[Category: Boehringer J]]
-[[Category: Endicott, J A]]
+[[Category: Brown NR]]
-[[Category: Gehring, K]]
+[[Category: Endicott JA]]
-[[Category: Gordon, C]]
+[[Category: Gehring K]]
-[[Category: Lowe, E D]]
+[[Category: Gordon C]]
-[[Category: Noble, M E.M]]
+[[Category: Lowe ED]]
-[[Category: Riedinger, C]]
+[[Category: Noble MEM]]
-[[Category: Trempe, J F]]
+[[Category: Riedinger C]]
-[[Category: Nuclear protein]]
+[[Category: Trempe J-F]]
-[[Category: Nucleus]]
-[[Category: Proteasome]]
-[[Category: Ubiquitin]]

2x5n

From Proteopedia

Current revision

Crystal Structure of the SpRpn10 VWA domain

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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