1k32: Difference between revisions

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 <StructureSection load='1k32' size='340' side='right'caption='[[1k32]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1k32]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/"thermoplasma_acidophila"_(sic)_darland_et_al._1970 "thermoplasma acidophila" (sic) darland et al. 1970]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K32 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1K32 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1k32]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K32 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K32 FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TA1490 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2303 "Thermoplasma acidophila" (sic) Darland et al. 1970])</td></tr>
+</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&#8491;</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1k32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k32 OCA], [http://pdbe.org/1k32 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1k32 RCSB], [http://www.ebi.ac.uk/pdbsum/1k32 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1k32 ProSAT]</span></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=1k32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k32 OCA], [https://pdbe.org/1k32 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k32 RCSB], [https://www.ebi.ac.uk/pdbsum/1k32 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k32 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/TRI_THEAC TRI_THEAC]] Tricorn degrades oligopeptides (probably derived from the proteasome) and channels the products to F1, F2 and F3 proteases, which then catalyze the terminal degradation step, yielding free amino acids.
+[https://www.uniprot.org/uniprot/TRI_THEAC TRI_THEAC] Tricorn degrades oligopeptides (probably derived from the proteasome) and channels the products to F1, F2 and F3 proteases, which then catalyze the terminal degradation step, yielding free amino acids.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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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=1k32 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The degradation of cytosolic proteins is carried out predominantly by the proteasome, which generates peptides of 7-9 amino acids long. These products need further processing. Recently, a proteolytic system was identified in the model organism Thermoplasma acidophilum that performs this processing. The hexameric core protein of this modular system, referred to as tricorn protease, is a 720K protease that is able to assemble further into a giant icosahedral capsid, as determined by electron microscopy. Here, we present the crystal structure of the tricorn protease at 2.0 A resolution. The structure reveals a complex mosaic protein whereby five domains combine to form one of six subunits, which further assemble to form the 3-2-symmetric core protein. The structure shows how the individual domains coordinate the specific steps of substrate processing, including channelling of the substrate to, and the product from, the catalytic site. Moreover, the structure shows how accessory protein components might contribute to an even more complex protein machinery that efficiently collects the tricorn-released products.
-Crystal structure of the tricorn protease reveals a protein disassembly line.,Brandstetter H, Kim JS, Groll M, Huber R Nature. 2001 Nov 22;414(6862):466-70. PMID:11719810<ref>PMID:11719810</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1k32" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Brandstetter, H]]
+[[Category: Thermoplasma acidophilum]]
-[[Category: Groll, M]]
+[[Category: Brandstetter H]]
-[[Category: Huber, R]]
+[[Category: Groll M]]
-[[Category: Kim, J S]]
+[[Category: Huber R]]
-[[Category: Beta propeller]]
+[[Category: Kim J-S]]
-[[Category: Hydrolase]]
-[[Category: Proteasome]]
-[[Category: Protein degradation]]
-[[Category: Serine protease]]
-[[Category: Substrate gating]]