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==== | ==Allosteric coupling between alpha-rings of 20S proteasome, 20S proteasome singly capped with a PA26/E102A_PANc, together with LFP incubation== | ||
<StructureSection load='6uth' size='340' side='right'caption='[[6uth]]' scene=''> | <StructureSection load='6uth' size='340' side='right'caption='[[6uth]], [[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'>[[6uth]] is a 35 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum] and [https://en.wikipedia.org/wiki/Trypanosoma_brucei Trypanosoma brucei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UTH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6UTH 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=6uth FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6uth OCA], [https://pdbe.org/6uth PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6uth RCSB], [https://www.ebi.ac.uk/pdbsum/6uth PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6uth 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: Trypanosoma brucei]] | |||
[[Category: Cheng Y]] | |||
[[Category: Yu Z]] | |||
Latest revision as of 17:33, 6 March 2024
Allosteric coupling between alpha-rings of 20S proteasome, 20S proteasome singly capped with a PA26/E102A_PANc, together with LFP incubationAllosteric coupling between alpha-rings of 20S proteasome, 20S proteasome singly capped with a PA26/E102A_PANc, together with LFP incubation
Structural highlights
FunctionPSA_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.[1] See AlsoReferences |
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