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| | ==Crystal Structure of a Novel Chaperone Complex for Yeast 20S Proteasome Assembly== | | ==Crystal Structure of a Novel Chaperone Complex for Yeast 20S Proteasome Assembly== |
| - | <StructureSection load='2z5c' size='340' side='right' caption='[[2z5c]], [[Resolution|resolution]] 2.90Å' scene=''> | + | <StructureSection load='2z5c' size='340' side='right'caption='[[2z5c]], [[Resolution|resolution]] 2.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2z5c]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z5C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Z5C FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2z5c]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z5C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Z5C FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2z5b|2z5b]]</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]] 2.9Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Proteasome_endopeptidase_complex Proteasome endopeptidase complex], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.25.1 3.4.25.1] </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=2z5c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z5c OCA], [https://pdbe.org/2z5c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2z5c RCSB], [https://www.ebi.ac.uk/pdbsum/2z5c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2z5c ProSAT]</span></td></tr> |
| - | <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=2z5c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z5c OCA], [http://pdbe.org/2z5c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2z5c RCSB], [http://www.ebi.ac.uk/pdbsum/2z5c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2z5c ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/POC4_YEAST POC4_YEAST]] Involved in 20S proteasome assembly, facilitating the alpha-ring formation. Involved in maintenance of telomere length.<ref>PMID:15161972</ref> <ref>PMID:17707236</ref> <ref>PMID:18278057</ref> [[http://www.uniprot.org/uniprot/PSA5_YEAST 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. [[http://www.uniprot.org/uniprot/POC3_YEAST POC3_YEAST]] Involved in 20S proteasome assembly, facilitating the alpha-ring formation.<ref>PMID:17707236</ref> <ref>PMID:18278057</ref> | + | [https://www.uniprot.org/uniprot/POC4_YEAST POC4_YEAST] Involved in 20S proteasome assembly, facilitating the alpha-ring formation. Involved in maintenance of telomere length.<ref>PMID:15161972</ref> <ref>PMID:17707236</ref> <ref>PMID:18278057</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/z5/2z5c_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/z5/2z5c_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | + | [[Category: Large Structures]] |
| - | [[Category: Proteasome endopeptidase complex]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Hayashi, H]] | + | [[Category: Hayashi H]] |
| - | [[Category: Hirano, Y]] | + | [[Category: Hirano Y]] |
| - | [[Category: Kameyama, T]] | + | [[Category: Kameyama T]] |
| - | [[Category: Kasahara, M]] | + | [[Category: Kasahara M]] |
| - | [[Category: Kato, K]] | + | [[Category: Kato K]] |
| - | [[Category: Kishimoto, T]] | + | [[Category: Kishimoto T]] |
| - | [[Category: Kurimoto, E]] | + | [[Category: Kurimoto E]] |
| - | [[Category: Mizushima, T]] | + | [[Category: Mizushima T]] |
| - | [[Category: Murata, S]] | + | [[Category: Murata S]] |
| - | [[Category: Okamoto, K]] | + | [[Category: Okamoto K]] |
| - | [[Category: Sakata, E]] | + | [[Category: Sakata E]] |
| - | [[Category: Suzuki, A]] | + | [[Category: Suzuki A]] |
| - | [[Category: Tanaka, K]] | + | [[Category: Tanaka K]] |
| - | [[Category: Yamane, T]] | + | [[Category: Yamane T]] |
| - | [[Category: Yashiroda, H]] | + | [[Category: Yashiroda H]] |
| - | [[Category: Chaperone]]
| + | |
| - | [[Category: Chaperone-hydrolase complex]]
| + | |
| - | [[Category: Proteasome]]
| + | |
| - | [[Category: S. cerevisiae]]
| + | |
| Structural highlights
Function
POC4_YEAST Involved in 20S proteasome assembly, facilitating the alpha-ring formation. Involved in maintenance of telomere length.[1] [2] [3]
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
Eukaryotic 20S proteasomes are composed of two alpha-rings and two beta-rings, which form an alphabetabetaalpha stacked structure. Here we describe a proteasome-specific chaperone complex, designated Dmp1-Dmp2, in budding yeast. Dmp1-Dmp2 directly bound to the alpha5 subunit to facilitate alpha-ring formation. In Deltadmp1 cells, alpha-rings lacking alpha4 and decreased formation of 20S proteasomes were observed. Dmp1-Dmp2 interacted with proteasome precursors early during proteasome assembly and dissociated from the precursors before the formation of half-proteasomes. Notably, the crystallographic structures of Dmp1 and Dmp2 closely resemble that of PAC3-a mammalian proteasome-assembling chaperone; nonetheless, neither Dmp1 nor Dmp2 showed obvious sequence similarity to PAC3. The structure of the Dmp1-Dmp2-alpha5 complex reveals how this chaperone functions in proteasome assembly and why it dissociates from proteasome precursors before the beta-rings are assembled.
Crystal structure of a chaperone complex that contributes to the assembly of yeast 20S proteasomes.,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 Nat Struct Mol Biol. 2008 Mar;15(3):228-36. Epub 2008 Feb 17. PMID:18278057[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
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