3vl1

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[[Image:3vl1.png|left|200px]]
 
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{{STRUCTURE_3vl1| PDB=3vl1 | SCENE= }}
{{STRUCTURE_3vl1| PDB=3vl1 | SCENE= }}
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===Crystal structure of yeast Rpn14===
===Crystal structure of yeast Rpn14===
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{{ABSTRACT_PUBMED_22691779}}
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==Function==
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[[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>
==About this Structure==
==About this Structure==
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[[3vl1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VL1 OCA].
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[[3vl1]] is a 2 chain structure with sequence from [http://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].
==See Also==
==See Also==
*[[Proteasome|Proteasome]]
*[[Proteasome|Proteasome]]
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[[Category: Saccharomyces cerevisiae]]
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==Reference==
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<ref group="xtra">PMID:022691779</ref><references group="xtra"/><references/>
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[[Category: Saccharomyces cerevisiae s288c]]
[[Category: Kato, K.]]
[[Category: Kato, K.]]
[[Category: Kim, S.]]
[[Category: Kim, S.]]

Revision as of 06:39, 14 August 2013

Template:STRUCTURE 3vl1

Contents

Crystal structure of yeast Rpn14

Template:ABSTRACT PUBMED 22691779

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]

About this Structure

3vl1 is a 2 chain structure with sequence from Saccharomyces cerevisiae s288c. Full crystallographic information is available from OCA.

See Also

Reference

  • 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. ↑ 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
  2. ↑ 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
  3. ↑ 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
  4. ↑ 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

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