2z5b
From Proteopedia
(Difference between revisions)
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<StructureSection load='2z5b' size='340' side='right'caption='[[2z5b]], [[Resolution|resolution]] 1.96Å' scene=''> | <StructureSection load='2z5b' size='340' side='right'caption='[[2z5b]], [[Resolution|resolution]] 1.96Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2z5b]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2z5b]] is a 2 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=2Z5B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Z5B FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.96Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2z5b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z5b OCA], [https://pdbe.org/2z5b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2z5b RCSB], [https://www.ebi.ac.uk/pdbsum/2z5b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2z5b ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [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]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2z5b ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2z5b ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == 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. | ||
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| - | 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<ref>PMID:18278057</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2z5b" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Atcc 18824]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Hayashi | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Hirano | + | [[Category: Hayashi H]] |
| - | [[Category: Kameyama | + | [[Category: Hirano Y]] |
| - | [[Category: Kasahara | + | [[Category: Kameyama T]] |
| - | [[Category: Kato | + | [[Category: Kasahara M]] |
| - | [[Category: Kishimoto | + | [[Category: Kato K]] |
| - | [[Category: Kurimoto | + | [[Category: Kishimoto T]] |
| - | [[Category: Mizushima | + | [[Category: Kurimoto E]] |
| - | [[Category: Murata | + | [[Category: Mizushima T]] |
| - | [[Category: Okamoto | + | [[Category: Murata S]] |
| - | [[Category: Sakata | + | [[Category: Okamoto K]] |
| - | [[Category: Suzuki | + | [[Category: Sakata E]] |
| - | [[Category: Tanaka | + | [[Category: Suzuki A]] |
| - | [[Category: Yamane | + | [[Category: Tanaka K]] |
| - | [[Category: Yashiroda | + | [[Category: Yamane T]] |
| - | + | [[Category: Yashiroda H]] | |
| - | + | ||
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Current revision
Crystal Structure of a Novel Chaperone Complex for Yeast 20S Proteasome Assembly
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Categories: Large Structures | Saccharomyces cerevisiae | Hayashi H | Hirano Y | Kameyama T | Kasahara M | Kato K | Kishimoto T | Kurimoto E | Mizushima T | Murata S | Okamoto K | Sakata E | Suzuki A | Tanaka K | Yamane T | Yashiroda H
