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[[Image:1j2q.gif|left|200px]]


{{Structure
==20S proteasome in complex with calpain-Inhibitor I from archaeoglobus fulgidus==
|PDB= 1j2q |SIZE=350|CAPTION= <scene name='initialview01'>1j2q</scene>, resolution 2.83&Aring;
<StructureSection load='1j2q' size='340' side='right'caption='[[1j2q]], [[Resolution|resolution]] 2.83&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CIB:2-ACETYLAMINO-4-METHYL-PENTANOIC+ACID+[1-(1-FORMYL-PENTYLCARBAMOYL)-3-METHYL-BUTYL]-AMIDE'>CIB</scene>
<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>
|ACTIVITY= <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='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>
|GENE=
<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>
|DOMAIN=
<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>
|RELATEDENTRY=[[1j2p|1J2P]]
</table>
|RESOURCES=<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://www.ebi.ac.uk/pdbsum/1j2q PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1j2q RCSB]</span>
== 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.


'''20S proteasome in complex with calpain-Inhibitor I from archaeoglobus fulgidus'''
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>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1j2q" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
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.
*[[Proteasome 3D structures|Proteasome 3D structures]]
 
== References ==
==About this Structure==
<references/>
1J2Q 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].
__TOC__
 
</StructureSection>
==Reference==
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]
[[Category: Archaeoglobus fulgidus]]
[[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]]
 
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