1j2q: Difference between revisions
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==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]] 2.83Å' scene=''> | <StructureSection load='1j2q' size='340' side='right' caption='[[1j2q]], [[Resolution|resolution]] 2.83Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1j2p|1j2p]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1j2p|1j2p]]</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='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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1j2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j2q OCA], [http://pdbe.org/1j2q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1j2q RCSB], [http://www.ebi.ac.uk/pdbsum/1j2q PDBsum]</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=1j2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j2q OCA], [http://pdbe.org/1j2q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1j2q RCSB], [http://www.ebi.ac.uk/pdbsum/1j2q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1j2q ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/j2/1j2q_consurf.spt"</scriptWhenChecked> | <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/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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</div> | </div> | ||
<div class="pdbe-citations 1j2q" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1j2q" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 12:06, 17 January 2018
20S proteasome in complex with calpain-Inhibitor I from archaeoglobus fulgidus20S proteasome in complex with calpain-Inhibitor I from archaeoglobus fulgidus
Structural highlights
Function[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] [PSB_ARCFU] Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation (By similarity).[HAMAP-Rule:MF_02113_A] 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 PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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