2z5c

Structural highlights

Function

[POC4_YEAST] Involved in 20S proteasome assembly, facilitating the alpha-ring formation. Involved in maintenance of telomere length.^{[1] [2] [3]} [PSA5_YEAST] The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity. [POC3_YEAST] Involved in 20S proteasome assembly, facilitating the alpha-ring formation.^{[4] [5]}

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

1. ↑ Askree SH, Yehuda T, Smolikov S, Gurevich R, Hawk J, Coker C, Krauskopf A, Kupiec M, McEachern MJ. A genome-wide screen for Saccharomyces cerevisiae deletion mutants that affect telomere length. Proc Natl Acad Sci U S A. 2004 Jun 8;101(23):8658-63. Epub 2004 May 25. PMID:15161972 doi:http://dx.doi.org/10.1073/pnas.0401263101
2. ↑ Le Tallec B, Barrault MB, Courbeyrette R, Guerois R, Marsolier-Kergoat MC, Peyroche A. 20S proteasome assembly is orchestrated by two distinct pairs of chaperones in yeast and in mammals. Mol Cell. 2007 Aug 17;27(4):660-74. PMID:17707236 doi:10.1016/j.molcel.2007.06.025
3. ↑ Yashiroda H, Mizushima T, Okamoto K, Kameyama T, Hayashi H, Kishimoto T, Niwa S, Kasahara M, Kurimoto E, Sakata E, Takagi K, Suzuki A, Hirano Y, Murata S, Kato K, Yamane T, Tanaka K. Crystal structure of a chaperone complex that contributes to the assembly of yeast 20S proteasomes. Nat Struct Mol Biol. 2008 Mar;15(3):228-36. Epub 2008 Feb 17. PMID:18278057 doi:http://dx.doi.org/10.1038/nsmb.1386
4. ↑ Le Tallec B, Barrault MB, Courbeyrette R, Guerois R, Marsolier-Kergoat MC, Peyroche A. 20S proteasome assembly is orchestrated by two distinct pairs of chaperones in yeast and in mammals. Mol Cell. 2007 Aug 17;27(4):660-74. PMID:17707236 doi:10.1016/j.molcel.2007.06.025
5. ↑ Yashiroda H, Mizushima T, Okamoto K, Kameyama T, Hayashi H, Kishimoto T, Niwa S, Kasahara M, Kurimoto E, Sakata E, Takagi K, Suzuki A, Hirano Y, Murata S, Kato K, Yamane T, Tanaka K. Crystal structure of a chaperone complex that contributes to the assembly of yeast 20S proteasomes. Nat Struct Mol Biol. 2008 Mar;15(3):228-36. Epub 2008 Feb 17. PMID:18278057 doi:http://dx.doi.org/10.1038/nsmb.1386
6. ↑ Yashiroda H, Mizushima T, Okamoto K, Kameyama T, Hayashi H, Kishimoto T, Niwa S, Kasahara M, Kurimoto E, Sakata E, Takagi K, Suzuki A, Hirano Y, Murata S, Kato K, Yamane T, Tanaka K. Crystal structure of a chaperone complex that contributes to the assembly of yeast 20S proteasomes. Nat Struct Mol Biol. 2008 Mar;15(3):228-36. Epub 2008 Feb 17. PMID:18278057 doi:http://dx.doi.org/10.1038/nsmb.1386