6uti
From Proteopedia
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| - | ==== | + | ==Allosteric coupling between alpha-rings of 20S proteasome, 20S proteasome with singly capped PAN complex== |
| - | <StructureSection load='6uti' size='340' side='right'caption='[[6uti]]' scene=''> | + | <StructureSection load='6uti' size='340' side='right'caption='[[6uti]], [[Resolution|resolution]] 3.40Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[6uti]] is a 28 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=6UTI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6UTI FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.4Å</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=6uti FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6uti OCA], [https://pdbe.org/6uti PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6uti RCSB], [https://www.ebi.ac.uk/pdbsum/6uti PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6uti ProSAT]</span></td></tr> | ||
</table> | </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> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Proteasome 3D structures|Proteasome 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Z | + | [[Category: Thermoplasma acidophilum]] |
| + | [[Category: Cheng Y]] | ||
| + | [[Category: Yu Z]] | ||
Revision as of 14:33, 6 March 2024
Allosteric coupling between alpha-rings of 20S proteasome, 20S proteasome with singly capped PAN complex
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