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3vl1

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Revision as of 08:03, 25 December 2014

Crystal structure of yeast Rpn14

Structural highlights

3vl1 is a 2 chain structure with sequence from Saccharomyces cerevisiae s288c. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	3acp
Gene:	RPN14 (Saccharomyces cerevisiae S288c)
Resources:	FirstGlance, OCA, RCSB, PDBsum

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.

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

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3vl1"

@@ Line 7: / Line 7: @@
 <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=3vl1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vl1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vl1 RCSB], [http://www.ebi.ac.uk/pdbsum/3vl1 PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://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;">
 == Publication Abstract from PubMed ==

3vl1

From Proteopedia

Revision as of 08:03, 25 December 2014

Crystal structure of yeast Rpn14

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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