1j2q: Difference between revisions

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-[[Image:1j2q.gif|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_1j2q", creates the "Structure Box" on the page.
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-or leave the SCENE parameter empty for the default display.
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-{{STRUCTURE_1j2q|  PDB=1j2q  |  SCENE=  }}
-'''20S proteasome in complex with calpain-Inhibitor I from archaeoglobus fulgidus'''
+==20S proteasome in complex with calpain-Inhibitor I from archaeoglobus fulgidus==
+<StructureSection load='1j2q' size='340' side='right'caption='[[1j2q]], [[Resolution|resolution]] 2.83&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1j2q]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J2Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1J2Q FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.83&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIB:2-ACETYLAMINO-4-METHYL-PENTANOIC+ACID+[1-(1-FORMYL-PENTYLCARBAMOYL)-3-METHYL-BUTYL]-AMIDE'>CIB</scene></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=1j2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j2q OCA], [https://pdbe.org/1j2q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j2q RCSB], [https://www.ebi.ac.uk/pdbsum/1j2q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j2q ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/PSA_ARCFU PSA_ARCFU] Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation (By similarity).[HAMAP-Rule:MF_00289_A]
+== 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/j2/1j2q_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1j2q ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The 20S proteasome (core particle, CP) is a multifunctional protease complex and composed of four heptameric subunit rings arranged in a hollow, barrel-shaped structure. Here, we report the crystal structure of the CP from Archaeoglobus fulgidus at 2.25A resolution. The analysis of the structure of early and late assembly intermediates of this CP gives new insights in the maturation of archaebacterial CPs and indicates similarities to assembly intermediates observed in eukaryotes. We also show a striking difference in mechanism and regulation of substrate access between eukaryotic and archaebacterial 20S proteasomes. While eukaryotic CPs are auto-inhibited by the N-terminal tails of the outer alpha-ring by imposing topological closure with a characteristic sequence motif (YDR-motif) and show regulatory gating this segment is disordered in the CP and differently structured in the alpha(7)-sub-complex of A.fulgidus leaving a pore leading into the particle with a diameter of 13A. Mutagenesis and functional studies indicate the absence of regulatory gating in the archaeal 20S proteasome.
-==Overview==
+Investigations on the maturation and regulation of archaebacterial proteasomes.,Groll M, Brandstetter H, Bartunik H, Bourenkow G, Huber R J Mol Biol. 2003 Mar 14;327(1):75-83. PMID:12614609<ref>PMID:12614609</ref>
-The 20S proteasome (core particle, CP) is a multifunctional protease complex and composed of four heptameric subunit rings arranged in a hollow, barrel-shaped structure. Here, we report the crystal structure of the CP from Archaeoglobus fulgidus at 2.25A resolution. The analysis of the structure of early and late assembly intermediates of this CP gives new insights in the maturation of archaebacterial CPs and indicates similarities to assembly intermediates observed in eukaryotes. We also show a striking difference in mechanism and regulation of substrate access between eukaryotic and archaebacterial 20S proteasomes. While eukaryotic CPs are auto-inhibited by the N-terminal tails of the outer alpha-ring by imposing topological closure with a characteristic sequence motif (YDR-motif) and show regulatory gating this segment is disordered in the CP and differently structured in the alpha(7)-sub-complex of A.fulgidus leaving a pore leading into the particle with a diameter of 13A. Mutagenesis and functional studies indicate the absence of regulatory gating in the archaeal 20S proteasome.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-J2Q is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J2Q OCA].
+</div>
+<div class="pdbe-citations 1j2q" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-Investigations on the maturation and regulation of archaebacterial proteasomes., Groll M, Brandstetter H, Bartunik H, Bourenkow G, Huber R, J Mol Biol. 2003 Mar 14;327(1):75-83. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12614609 12614609]
+*[[Proteasome 3D structures|Proteasome 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Archaeoglobus fulgidus]]
-[[Category: Proteasome endopeptidase complex]]
+[[Category: Large Structures]]
-[[Category: Protein complex]]
+[[Category: Bartunik H]]
-[[Category: Bartunik, H.]]
+[[Category: Bourenkow G]]
-[[Category: Bourenkow, G.]]
+[[Category: Brandstetter H]]
-[[Category: Brandstetter, H.]]
+[[Category: Groll M]]
-[[Category: Groll, M.]]
+[[Category: Huber R]]
-[[Category: Huber, R.]]
-[[Category: 20]]
-[[Category: Cp]]
-[[Category: Proteasome]]
-[[Category: Ubiquitin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 20:43:56 2008''