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| | <StructureSection load='3vl1' size='340' side='right'caption='[[3vl1]], [[Resolution|resolution]] 1.60Å' scene=''> | | <StructureSection load='3vl1' size='340' side='right'caption='[[3vl1]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3vl1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VL1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VL1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3vl1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VL1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VL1 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3acp|3acp]]</div></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]] 1.6Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RPN14 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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=3vl1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vl1 OCA], [https://pdbe.org/3vl1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vl1 RCSB], [https://www.ebi.ac.uk/pdbsum/3vl1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vl1 ProSAT]</span></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=3vl1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vl1 OCA], [https://pdbe.org/3vl1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vl1 RCSB], [https://www.ebi.ac.uk/pdbsum/3vl1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vl1 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/RPN14_YEAST RPN14_YEAST]] Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. Is not a genuine component of the 26S proteasome, but an auxiliary factor that interacts with the proteasomal ATPase of 19S regulatory particle (RP). Acts as a chaperone which regulates the highly structured assembly of the 19S regulatory particle. Involved in the substrate specificity of the 26S proteasome and is especially involved in the degradation of ubiquitinated GCN4. May contribute to the stability of the 26S proteasome in some stress conditions.<ref>PMID:17499717</ref> <ref>PMID:19412159</ref> <ref>PMID:19446322</ref> <ref>PMID:19446323</ref>
| + | [https://www.uniprot.org/uniprot/RPN14_YEAST RPN14_YEAST] Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. Is not a genuine component of the 26S proteasome, but an auxiliary factor that interacts with the proteasomal ATPase of 19S regulatory particle (RP). Acts as a chaperone which regulates the highly structured assembly of the 19S regulatory particle. Involved in the substrate specificity of the 26S proteasome and is especially involved in the degradation of ubiquitinated GCN4. May contribute to the stability of the 26S proteasome in some stress conditions.<ref>PMID:17499717</ref> <ref>PMID:19412159</ref> <ref>PMID:19446322</ref> <ref>PMID:19446323</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Baker's yeast]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kato, K]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Kim, S]] | + | [[Category: Kato K]] |
| - | [[Category: Mizushima, T]] | + | [[Category: Kim S]] |
| - | [[Category: Nishide, A]] | + | [[Category: Mizushima T]] |
| - | [[Category: Saeki, Y]] | + | [[Category: Nishide A]] |
| - | [[Category: Takagi, K]] | + | [[Category: Saeki Y]] |
| - | [[Category: Tanaka, K]] | + | [[Category: Takagi K]] |
| - | [[Category: Beta-propeller]]
| + | [[Category: Tanaka K]] |
| - | [[Category: Chaperone]]
| + | |
| - | [[Category: Rpt6]]
| + | |
| Structural highlights
Function
RPN14_YEAST Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. Is not a genuine component of the 26S proteasome, but an auxiliary factor that interacts with the proteasomal ATPase of 19S regulatory particle (RP). Acts as a chaperone which regulates the highly structured assembly of the 19S regulatory particle. Involved in the substrate specificity of the 26S proteasome and is especially involved in the degradation of ubiquitinated GCN4. May contribute to the stability of the 26S proteasome in some stress conditions.[1] [2] [3] [4]
Publication Abstract from PubMed
The 26S proteasome is an ATP-dependent protease responsible for selective degradation of polyubiquitylated proteins. Recent studies have suggested that proteasome assembly is a highly ordered multi-step process assisted by specific chaperones. Rpn14, an assembly chaperone for ATPase-ring formation, specifically recognizes the ATPase subunit Rpt6. The structure of Rpn14 at 2.0 A resolution in space group P6(4) has previously been reported, but the detailed mechanism of Rpn14 function remains unclear. Here, a new crystal structure of Rpn14 with an E384A mutation is presented in space group P2(1) at 1.6 A resolution. This high-resolution structure provides a framework for understanding proteasome assembly.
New crystal structure of the proteasome-dedicated chaperone Rpn14 at 1.6 A resolution.,Kim S, Nishide A, Saeki Y, Takagi K, Tanaka K, Kato K, Mizushima T Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 May 1;68(Pt 5):517-21., doi: 10.1107/S1744309112011359. Epub 2012 Apr 20. PMID:22691779[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Seong KM, Baek JH, Yu MH, Kim J. Rpn13p and Rpn14p are involved in the recognition of ubiquitinated Gcn4p by the 26S proteasome. FEBS Lett. 2007 May 29;581(13):2567-73. Epub 2007 Apr 30. PMID:17499717 doi:10.1016/j.febslet.2007.04.064
- ↑ Roelofs J, Park S, Haas W, Tian G, McAllister FE, Huo Y, Lee BH, Zhang F, Shi Y, Gygi SP, Finley D. Chaperone-mediated pathway of proteasome regulatory particle assembly. Nature. 2009 Jun 11;459(7248):861-5. PMID:19412159 doi:nature08063
- ↑ Funakoshi M, Tomko RJ Jr, Kobayashi H, Hochstrasser M. Multiple assembly chaperones govern biogenesis of the proteasome regulatory particle base. Cell. 2009 May 29;137(5):887-99. Epub 2009 May 14. PMID:19446322 doi:S0092-8674(09)00526-1
- ↑ Saeki Y, Toh-E A, Kudo T, Kawamura H, Tanaka K. Multiple proteasome-interacting proteins assist the assembly of the yeast 19S regulatory particle. Cell. 2009 May 29;137(5):900-13. Epub 2009 May 14. PMID:19446323 doi:S0092-8674(09)00528-5
- ↑ Kim S, Nishide A, Saeki Y, Takagi K, Tanaka K, Kato K, Mizushima T. New crystal structure of the proteasome-dedicated chaperone Rpn14 at 1.6 A resolution. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 May 1;68(Pt 5):517-21., doi: 10.1107/S1744309112011359. Epub 2012 Apr 20. PMID:22691779 doi:10.1107/S1744309112011359
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