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| | <StructureSection load='3ipm' size='340' side='right'caption='[[3ipm]], [[Resolution|resolution]] 4.00Å' scene=''> | | <StructureSection load='3ipm' size='340' side='right'caption='[[3ipm]], [[Resolution|resolution]] 4.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3ipm]] 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/Tryb2 Tryb2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IPM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IPM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3ipm]] is a 21 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii], [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=3IPM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IPM FirstGlance]. <br> |
| - | </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]), Tb10.70.3660 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=185431 TRYB2])</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]] 4Å</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=3ipm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ipm OCA], [https://pdbe.org/3ipm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ipm RCSB], [https://www.ebi.ac.uk/pdbsum/3ipm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ipm 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=3ipm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ipm OCA], [https://pdbe.org/3ipm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ipm RCSB], [https://www.ebi.ac.uk/pdbsum/3ipm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ipm 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: Methanocaldococcus jannaschii]] |
| - | [[Category: Tryb2]] | + | [[Category: Thermoplasma acidophilum]] |
| - | [[Category: Cheng, Y]] | + | [[Category: Trypanosoma brucei]] |
| - | [[Category: Yu, Y]] | + | [[Category: Cheng Y]] |
| - | [[Category: Aaa atpase]] | + | [[Category: Yu Y]] |
| - | [[Category: Electron cryomicroscopy]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Hydrolase-hydrolase activator complex]]
| + | |
| - | [[Category: Protease]]
| + | |
| - | [[Category: Proteasomal atpase]]
| + | |
| - | [[Category: Proteasome]]
| + | |
| - | [[Category: Protein degradation]]
| + | |
| - | [[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
Protein degradation in the 20S proteasome is regulated in eukaryotes by the 19S ATPase complex and in archaea by the homologous PAN ATPase ring complex. Subunits of these hexameric ATPases contain on their C-termini a conserved hydrophobic-tyrosine-X (HbYX) motif that docks into pockets in the 20S to stimulate the opening of a gated substrate entry channel. Here, we report the crystal structure of the archaeal 20S proteasome in complex with the C-terminus of the archaeal proteasome regulatory ATPase, PAN. This structure defines the detailed interactions between the critical C-terminal HbYX motif and the 20S alpha-subunits and indicates that the intersubunit pocket in the 20S undergoes an induced-fit conformational change on binding of the HbYX motif. This structure together with related mutagenesis data suggest how in eukaryotes certain proteasomal ATPases bind to specific pockets in an asymmetrical manner to regulate gate opening.
Interactions of PAN's C-termini with archaeal 20S proteasome and implications for the eukaryotic proteasome-ATPase interactions.,Yu Y, Smith DM, Kim HM, Rodriguez V, Goldberg AL, Cheng Y EMBO J. 2010 Feb 3;29(3):692-702. Epub 2009 Dec 17. PMID:20019667[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
- ↑ Yu Y, Smith DM, Kim HM, Rodriguez V, Goldberg AL, Cheng Y. Interactions of PAN's C-termini with archaeal 20S proteasome and implications for the eukaryotic proteasome-ATPase interactions. EMBO J. 2010 Feb 3;29(3):692-702. Epub 2009 Dec 17. PMID:20019667 doi:10.1038/emboj.2009.382
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