|
|
| Line 3: |
Line 3: |
| | <SX load='6muw' size='340' side='right' viewer='molstar' caption='[[6muw]], [[Resolution|resolution]] 3.60Å' scene=''> | | <SX load='6muw' size='340' side='right' viewer='molstar' caption='[[6muw]], [[Resolution|resolution]] 3.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6muw]] is a 28 chain structure with sequence from [http://en.wikipedia.org/wiki/Plasmodium_falciparum_(isolate_3d7) Plasmodium falciparum (isolate 3d7)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MUW OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6MUW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6muw]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum_3D7 Plasmodium falciparum 3D7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MUW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MUW FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6mux|6mux]], [[6muv|6muv]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.6Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Proteasome_endopeptidase_complex Proteasome endopeptidase complex], with EC number [http://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=6muw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6muw OCA], [https://pdbe.org/6muw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6muw RCSB], [https://www.ebi.ac.uk/pdbsum/6muw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6muw ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6muw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6muw OCA], [http://pdbe.org/6muw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6muw RCSB], [http://www.ebi.ac.uk/pdbsum/6muw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6muw ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/Q8IKC9_PLAF7 Q8IKC9_PLAF7]] The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.[RuleBase:RU004203] [[http://www.uniprot.org/uniprot/Q8IDG3_PLAF7 Q8IDG3_PLAF7]] The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH.[RuleBase:RU000551] [[http://www.uniprot.org/uniprot/Q8I6T3_PLAF7 Q8I6T3_PLAF7]] The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.[RuleBase:RU004203] [[http://www.uniprot.org/uniprot/Q8IJT1_PLAF7 Q8IJT1_PLAF7]] The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.[RuleBase:RU004203] [[http://www.uniprot.org/uniprot/Q7K6A9_PLAF7 Q7K6A9_PLAF7]] The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.[RuleBase:RU004203] [[http://www.uniprot.org/uniprot/Q8IDG2_PLAF7 Q8IDG2_PLAF7]] The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH.[RuleBase:RU000551] [[http://www.uniprot.org/uniprot/C0H4E8_PLAF7 C0H4E8_PLAF7]] The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.[RuleBase:RU004203] [[http://www.uniprot.org/uniprot/Q8IBI3_PLAF7 Q8IBI3_PLAF7]] The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH.[RuleBase:RU000551] | + | [https://www.uniprot.org/uniprot/Q8IAR3_PLAF7 Q8IAR3_PLAF7] |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | The activity of the proteasome 20S catalytic core is regulated by protein complexes that bind to one or both ends. The PA28 regulator stimulates 20S proteasome peptidase activity in vitro, but its role in vivo remains unclear. Here, we show that genetic deletion of the PA28 regulator from Plasmodium falciparum (Pf) renders malaria parasites more sensitive to the antimalarial drug dihydroartemisinin, indicating that PA28 may play a role in protection against proteotoxic stress. The crystal structure of PfPA28 reveals a bell-shaped molecule with an inner pore that has a strong segregation of charges. Small-angle X-ray scattering shows that disordered loops, which are not resolved in the crystal structure, extend from the PfPA28 heptamer and surround the pore. Using single particle cryo-electron microscopy, we solved the structure of Pf20S in complex with one and two regulatory PfPA28 caps at resolutions of 3.9 and 3.8 A, respectively. PfPA28 binds Pf20S asymmetrically, strongly engaging subunits on only one side of the core. PfPA28 undergoes rigid body motions relative to Pf20S. Molecular dynamics simulations support conformational flexibility and a leaky interface. We propose lateral transfer of short peptides through the dynamic interface as a mechanism facilitating the release of proteasome degradation products.
| + | |
| - | | + | |
| - | The structure of the PA28-20S proteasome complex from Plasmodium falciparum and implications for proteostasis.,Xie SC, Metcalfe RD, Hanssen E, Yang T, Gillett DL, Leis AP, Morton CJ, Kuiper MJ, Parker MW, Spillman NJ, Wong W, Tsu C, Dick LR, Griffin MDW, Tilley L Nat Microbiol. 2019 Aug 5. pii: 10.1038/s41564-019-0524-4. doi:, 10.1038/s41564-019-0524-4. PMID:31384003<ref>PMID:31384003</ref>
| + | |
| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 6muw" style="background-color:#fffaf0;"></div>
| + | |
| | | | |
| | ==See Also== | | ==See Also== |
| | *[[Proteasome 3D structures|Proteasome 3D structures]] | | *[[Proteasome 3D structures|Proteasome 3D structures]] |
| - | == References == | |
| - | <references/> | |
| | __TOC__ | | __TOC__ |
| | </SX> | | </SX> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Proteasome endopeptidase complex]] | + | [[Category: Plasmodium falciparum 3D7]] |
| - | [[Category: Gillett, D L]] | + | [[Category: Gillett DL]] |
| - | [[Category: Griffin, M D.W]] | + | [[Category: Griffin MDW]] |
| - | [[Category: Hanssen, E]] | + | [[Category: Hanssen E]] |
| - | [[Category: Leis, A P]] | + | [[Category: Leis AP]] |
| - | [[Category: Metcalfe, R D]] | + | [[Category: Metcalfe RD]] |
| - | [[Category: Tilley, L]] | + | [[Category: Tilley L]] |
| - | [[Category: Xie, S C]] | + | [[Category: Xie SC]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Protease]]
| + | |
| - | [[Category: Proteasome]]
| + | |
