1k32: Difference between revisions

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-[[Image:1k32.gif|left|200px]]
-<!--
+==Crystal structure of the tricorn protease==
-The line below this paragraph, containing "STRUCTURE_1k32", creates the "Structure Box" on the page.
+<StructureSection load='1k32' size='340' side='right'caption='[[1k32]], [[Resolution|resolution]] 2.00&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'>[[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>
-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]] 2&#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=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>
-{{STRUCTURE_1k32|  PDB=1k32  |  SCENE=  }}
+</table>
+== Function ==
-'''Crystal structure of the tricorn protease'''
+[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]]
-==Overview==
+Check<jmol>
-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.
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k3/1k32_consurf.spt"</scriptWhenChecked>
-==About this Structure==
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
-K32 is a [[Single protein]] structure of sequence from [http://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].
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
-==Reference==
+</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].
-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:[http://www.ncbi.nlm.nih.gov/pubmed/11719810 11719810]
+<div style="clear:both"></div>
-[[Category: Single protein]]
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Thermoplasma acidophilum]]
-[[Category: Brandstetter, H.]]
+[[Category: Brandstetter H]]
-[[Category: Groll, M.]]
+[[Category: Groll M]]
-[[Category: Huber, R.]]
+[[Category: Huber R]]
-[[Category: Kim, J S.]]
+[[Category: Kim J-S]]
-[[Category: Beta propeller]]
-[[Category: Proteasome]]
-[[Category: Protein degradation]]
-[[Category: Serine protease]]
-[[Category: Substrate gating]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 22:14:29 2008''