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| | <StructureSection load='3jrm' size='340' side='right'caption='[[3jrm]], [[Resolution|resolution]] 2.90Å' scene=''> | | <StructureSection load='3jrm' size='340' side='right'caption='[[3jrm]], [[Resolution|resolution]] 2.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3jrm]] is a 21 chain structure with sequence from [https://en.wikipedia.org/wiki/"thermoplasma_acidophila"_(sic)_darland_et_al._1970 "thermoplasma acidophila" (sic) darland et al. 1970] and [https://en.wikipedia.org/wiki/Trypanosoma_(trypanozoon)_brucei Trypanosoma (trypanozoon) brucei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JRM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3JRM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3jrm]] is a 21 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=3JRM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3JRM 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;'>[[1ya7|1ya7]], [[3jse|3jse]], [[3jtl|3jtl]]</div></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]] 2.9Å</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]), psmB, Ta0612 ([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=3jrm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jrm OCA], [https://pdbe.org/3jrm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3jrm RCSB], [https://www.ebi.ac.uk/pdbsum/3jrm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3jrm 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=3jrm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jrm OCA], [https://pdbe.org/3jrm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3jrm RCSB], [https://www.ebi.ac.uk/pdbsum/3jrm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3jrm ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == 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/PSB_THEAC PSB_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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Proteasome endopeptidase complex]] | + | [[Category: Thermoplasma acidophilum]] |
| - | [[Category: Hill, C P]] | + | [[Category: Trypanosoma brucei]] |
| - | [[Category: Stadtmueller, B M]] | + | [[Category: Hill CP]] |
| - | [[Category: Whitby, F G]] | + | [[Category: Stadtmueller BM]] |
| - | [[Category: 20s proteasome]] | + | [[Category: Whitby FG]] |
| - | [[Category: Cytoplasm]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Hydrolase-hydrolase activator complex]]
| + | |
| - | [[Category: Pa26]]
| + | |
| - | [[Category: Protease]]
| + | |
| - | [[Category: Proteasome]]
| + | |
| - | [[Category: Threonine protease]]
| + | |
| Structural highlights
Function
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.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Proteasome activity is regulated by sequestration of its proteolytic centers in a barrel-shaped structure that limits substrate access. Substrates enter the proteasome by means of activator complexes that bind to the end rings of proteasome alpha subunits and induce opening of an axial entrance/exit pore. The PA26 activator binds in a pocket on the proteasome surface using main chain contacts of its C-terminal residues and uses an internal activation loop to trigger gate opening by repositioning the proteasome Pro-17 reverse turn. Subunits of the unrelated PAN/19S activators bind with their C termini in the same pockets but can induce proteasome gate opening entirely from interactions of their C-terminal peptides, which are reported to cause gate opening by inducing a rocking motion of proteasome alpha subunits rather than by directly contacting the Pro-17 turn. Here we report crystal structures and binding studies of proteasome complexes with PA26 constructs that display modified C-terminal residues, including those corresponding to PAN. These findings suggest that PA26 and PAN/19S C-terminal residues bind superimposably and that both classes of activator induce gate opening by using direct contacts to residues of the proteasome Pro-17 reverse turn. In the case of the PAN and 19S activators, a penultimate tyrosine/phenylalanine residue contacts the proteasome Gly-19 carbonyl oxygen to stabilize the open conformation.
Structural models for interactions between the 20S proteasome and its PAN/19S activators.,Stadtmueller BM, Ferrell K, Whitby FG, Heroux A, Robinson H, Myszka DG, Hill CP J Biol Chem. 2010 Jan 1;285(1):13-7. Epub 2009 Nov 4. PMID:19889631[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Akopian TN, Kisselev AF, Goldberg AL. Processive degradation of proteins and other catalytic properties of the proteasome from Thermoplasma acidophilum. J Biol Chem. 1997 Jan 17;272(3):1791-8. PMID:8999862
- ↑ Stadtmueller BM, Ferrell K, Whitby FG, Heroux A, Robinson H, Myszka DG, Hill CP. Structural models for interactions between the 20S proteasome and its PAN/19S activators. J Biol Chem. 2010 Jan 1;285(1):13-7. Epub 2009 Nov 4. PMID:19889631 doi:10.1074/jbc.C109.070425
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