1z7q: Difference between revisions

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-[[Image:1z7q.png|left|200px]]
-<!--
+==Crystal structure of the 20s proteasome from yeast in complex with the proteasome activator PA26 from Trypanosome brucei at 3.2 angstroms resolution==
-The line below this paragraph, containing "STRUCTURE_1z7q", creates the "Structure Box" on the page.
+<StructureSection load='1z7q' size='340' side='right'caption='[[1z7q]], [[Resolution|resolution]] 3.22&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1z7q]] is a 20 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=1Z7Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z7Q FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.22&#8491;</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=1z7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z7q OCA], [https://pdbe.org/1z7q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z7q RCSB], [https://www.ebi.ac.uk/pdbsum/1z7q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z7q ProSAT]</span></td></tr>
-{{STRUCTURE_1z7q|  PDB=1z7q  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/PSA1_YEAST PSA1_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.
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/z7/1z7q_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=1z7q ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Proteasomes are cylindrical structures that function in multiple cellular processes by degrading a wide variety of cytosolic and nuclear proteins. Substrate access and product release from the enclosed catalytic chamber occurs through axial pores that are opened by activator complexes. Here, we report high-resolution structures of wild-type and mutant archaeal proteasomes bound to the activator PA26. These structures support the proposal that an ordered open conformation is required for proteolysis and that its formation can be triggered by outward displacement of surrounding residues. The structures and associated biochemical assays reveal the mechanism of binding, which involves an interaction between the PA26 C terminus and a conserved lysine. Surprisingly, biochemical observations implicate an equivalent interaction for the unrelated ATP-dependent activators PAN and PA700.
-===Crystal structure of the 20s proteasome from yeast in complex with the proteasome activator PA26 from Trypanosome brucei at 3.2 angstroms resolution===
+The 1.9 A structure of a proteasome-11S activator complex and implications for proteasome-PAN/PA700 interactions.,Forster A, Masters EI, Whitby FG, Robinson H, Hill CP Mol Cell. 2005 May 27;18(5):589-99. PMID:15916965<ref>PMID:15916965</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_15916965}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1z7q" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 15916965 is the PubMed ID number.
--->
-{{ABSTRACT_PUBMED_15916965}}
-==About this Structure==
-[[1z7q]] is a 42 chain structure of [[Proteasome]] with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] and [http://en.wikipedia.org/wiki/Trypanosoma_brucei Trypanosoma brucei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z7Q OCA].
 ==See Also==
-*[[Proteasome|Proteasome]]
+*[[Proteasome 3D structures|Proteasome 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:015916965</ref><references group="xtra"/>
+__TOC__
-[[Category: Proteasome endopeptidase complex]]
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Saccharomyces cerevisiae]]
-[[Category: Trypanosoma brucei]]
+[[Category: Forster A]]
-[[Category: Forster, A.]]
+[[Category: Hill CP]]
-[[Category: Hill, C P.]]
+[[Category: Whitby FG]]
-[[Category: Whitby, F G.]]
-[[Category: 20]]
-[[Category: Activator]]
-[[Category: Hydrolase-hydrolase activator complex]]
-[[Category: Multi-catalytic protease]]
-[[Category: Pa26]]
-[[Category: Proteasome]]