2z5c

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[[Image:2z5c.jpg|left|200px]]
 
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==Crystal Structure of a Novel Chaperone Complex for Yeast 20S Proteasome Assembly==
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The line below this paragraph, containing "STRUCTURE_2z5c", creates the "Structure Box" on the page.
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<StructureSection load='2z5c' size='340' side='right'caption='[[2z5c]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
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<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>
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{{STRUCTURE_2z5c| PDB=2z5c | SCENE= }}
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</table>
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== Function ==
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'''Crystal Structure of a Novel Chaperone Complex for Yeast 20S Proteasome Assembly'''
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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==Overview==
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/z5/2z5c_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=2z5c ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== 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.
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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==About this Structure==
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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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2Z5C is a [[Protein complex]] structure of sequences 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=2Z5C OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://www.ncbi.nlm.nih.gov/pubmed/18278057 18278057]
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</div>
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[[Category: Proteasome endopeptidase complex]]
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<div class="pdbe-citations 2z5c" style="background-color:#fffaf0;"></div>
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[[Category: Protein complex]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Hayashi, H.]]
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[[Category: Hayashi H]]
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[[Category: Hirano, Y.]]
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[[Category: Hirano Y]]
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[[Category: Kameyama, T.]]
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[[Category: Kameyama T]]
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[[Category: Kasahara, M.]]
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[[Category: Kasahara M]]
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[[Category: Kato, K.]]
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[[Category: Kato K]]
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[[Category: Kishimoto, T.]]
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[[Category: Kishimoto T]]
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[[Category: Kurimoto, E.]]
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[[Category: Kurimoto E]]
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[[Category: Mizushima, T.]]
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[[Category: Mizushima T]]
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[[Category: Murata, S.]]
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[[Category: Murata S]]
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[[Category: Okamoto, K.]]
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[[Category: Okamoto K]]
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[[Category: Sakata, E.]]
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[[Category: Sakata E]]
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[[Category: Suzuki, A.]]
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[[Category: Suzuki A]]
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[[Category: Tanaka, K.]]
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[[Category: Tanaka K]]
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[[Category: Yamane, T.]]
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[[Category: Yamane T]]
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[[Category: Yashiroda, H.]]
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[[Category: Yashiroda H]]
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[[Category: Chaperone]]
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[[Category: Chaperone/hydrolase complex]]
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[[Category: Proteasome]]
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[[Category: S. cerevisiae]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 19:57:45 2008''
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Current revision

Crystal Structure of a Novel Chaperone Complex for Yeast 20S Proteasome Assembly

PDB ID 2z5c

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