2ku2: Difference between revisions

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OCA

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 ==Dynamic Regulation of Archaeal Proteasome Gate Opening as Studied by TROSY-NMR==
-<StructureSection load='2ku2' size='340' side='right'caption='[[2ku2]], [[NMR_Ensembles_of_Models | 50 NMR models]]' scene=''>
+<StructureSection load='2ku2' size='340' side='right'caption='[[2ku2]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2ku2]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/"thermoplasma_acidophila"_(sic)_darland_et_al._1970 "thermoplasma acidophila" (sic) darland et al. 1970]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KU2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KU2 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2ku2]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KU2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KU2 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1pma|1pma]], [[1ya7|1ya7]], [[2ku1|2ku1]]</div></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">psmA, Ta1288 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2303 "Thermoplasma acidophila" (sic) Darland et al. 1970])</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Proteasome_endopeptidase_complex Proteasome endopeptidase complex], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=2ku2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ku2 OCA], [https://pdbe.org/2ku2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ku2 RCSB], [https://www.ebi.ac.uk/pdbsum/2ku2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ku2 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/PSA_THEAC PSA_THEAC]] Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The T.acidophilum proteasome is able to cleave oligopeptides after Tyr, Leu, Phe, and to a lesser extent after Glu and Arg. Thus, displays chymotrypsin-like activity and low level of caspase-like and trypsin-like activities.<ref>PMID:8999862</ref>
+[https://www.uniprot.org/uniprot/PSA_THEAC PSA_THEAC] Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The T.acidophilum proteasome is able to cleave oligopeptides after Tyr, Leu, Phe, and to a lesser extent after Glu and Arg. Thus, displays chymotrypsin-like activity and low level of caspase-like and trypsin-like activities.<ref>PMID:8999862</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Proteasome endopeptidase complex]]
+[[Category: Thermoplasma acidophilum]]
-[[Category: Kay, L E]]
+[[Category: Kay LE]]
-[[Category: Religa, T L]]
+[[Category: Religa TL]]
-[[Category: Sprangers, R]]
+[[Category: Sprangers R]]
-[[Category: Cytoplasm]]
-[[Category: Gating residue]]
-[[Category: Hydrolase]]
-[[Category: Protease]]
-[[Category: Proteasome]]
-[[Category: Proteolysis]]
-[[Category: Threonine protease]]