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| | <StructureSection load='5lfq' size='340' side='right'caption='[[5lfq]], [[Resolution|resolution]] 3.50Å' scene=''> | | <StructureSection load='5lfq' size='340' side='right'caption='[[5lfq]], [[Resolution|resolution]] 3.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5lfq]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LFQ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5LFQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5lfq]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LFQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LFQ FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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]] 3.503Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5lfj|5lfj]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bpa, Rv3780, MTCY13D12.14 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</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=5lfq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lfq OCA], [https://pdbe.org/5lfq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lfq RCSB], [https://www.ebi.ac.uk/pdbsum/5lfq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lfq 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=5lfq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lfq OCA], [http://pdbe.org/5lfq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lfq RCSB], [http://www.ebi.ac.uk/pdbsum/5lfq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lfq ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/BPA_MYCTU BPA_MYCTU]] Interacts with the core proteasome alpha-subunit (PrcA) through its C-terminal hydrophobic-tyrosine-X motif (HbYX motif). Interaction of Bpa with the proteasome stimulates proteosomal peptidase and casein degradation activity, which suggests Bpa could play a role in the removal of non-native or damaged proteins by influencing the conformation of the proteasome complex upon interaction. Can inhibit degradation of Pup-tagged substrates in vitro by competing with Mpa for association with the proteasome.<ref>PMID:25469515</ref> | + | [https://www.uniprot.org/uniprot/BPA_MYCTU BPA_MYCTU] Interacts with the core proteasome alpha-subunit (PrcA) through its C-terminal hydrophobic-tyrosine-X motif (HbYX motif). Interaction of Bpa with the proteasome stimulates proteosomal peptidase and casein degradation activity, which suggests Bpa could play a role in the removal of non-native or damaged proteins by influencing the conformation of the proteasome complex upon interaction. Can inhibit degradation of Pup-tagged substrates in vitro by competing with Mpa for association with the proteasome.<ref>PMID:25469515</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Myctu]] | + | [[Category: Mycobacterium tuberculosis H37Rv]] |
| - | [[Category: Ban, N]] | + | [[Category: Ban N]] |
| - | [[Category: Boehringer, D]] | + | [[Category: Boehringer D]] |
| - | [[Category: Bolten, M]] | + | [[Category: Bolten M]] |
| - | [[Category: Delley, C L]] | + | [[Category: Delley CL]] |
| - | [[Category: Leibundgut, M]] | + | [[Category: Leibundgut M]] |
| - | [[Category: Weber-Ban, E]] | + | [[Category: Weber-Ban E]] |
| - | [[Category: Dodecamer]]
| + | |
| - | [[Category: Four-helix bundle]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| Structural highlights
Function
BPA_MYCTU Interacts with the core proteasome alpha-subunit (PrcA) through its C-terminal hydrophobic-tyrosine-X motif (HbYX motif). Interaction of Bpa with the proteasome stimulates proteosomal peptidase and casein degradation activity, which suggests Bpa could play a role in the removal of non-native or damaged proteins by influencing the conformation of the proteasome complex upon interaction. Can inhibit degradation of Pup-tagged substrates in vitro by competing with Mpa for association with the proteasome.[1]
Publication Abstract from PubMed
Mycobacterium tuberculosis harbors proteasomes that recruit substrates for degradation through an ubiquitin-like modification pathway. Recently, a non-ATPase activator termed Bpa (bacterial proteasome activator) was shown to support an alternate proteasomal degradation pathway. Here, we present the cryo-electron microscopy (cryo-EM) structure of Bpa in complex with the 20S core particle (CP). For docking into the cryo-EM density, we solved the X-ray structure of Bpa, showing that it forms tight four-helix bundles arranged into a 12-membered ring with a 40 A wide central pore and the C-terminal helix of each protomer protruding from the ring. The Bpa model was fitted into the cryo-EM map of the Bpa-CP complex, revealing its architecture and striking symmetry mismatch. The Bpa-CP interface was resolved to 3.5 A, showing the interactions between the C-terminal GQYL motif of Bpa and the proteasome alpha-rings. This docking mode is related to the one observed for eukaryotic activators with features specific to the bacterial complex.
Structural Analysis of the Bacterial Proteasome Activator Bpa in Complex with the 20S Proteasome.,Bolten M, Delley CL, Leibundgut M, Boehringer D, Ban N, Weber-Ban E Structure. 2016 Dec 6;24(12):2138-2151. doi: 10.1016/j.str.2016.10.008. Epub 2016, Nov 10. PMID:27839949[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Delley CL, Laederach J, Ziemski M, Bolten M, Boehringer D, Weber-Ban E. Bacterial proteasome activator bpa (rv3780) is a novel ring-shaped interactor of the mycobacterial proteasome. PLoS One. 2014 Dec 3;9(12):e114348. doi: 10.1371/journal.pone.0114348., eCollection 2014. PMID:25469515 doi:http://dx.doi.org/10.1371/journal.pone.0114348
- ↑ Bolten M, Delley CL, Leibundgut M, Boehringer D, Ban N, Weber-Ban E. Structural Analysis of the Bacterial Proteasome Activator Bpa in Complex with the 20S Proteasome. Structure. 2016 Dec 6;24(12):2138-2151. doi: 10.1016/j.str.2016.10.008. Epub 2016, Nov 10. PMID:27839949 doi:http://dx.doi.org/10.1016/j.str.2016.10.008
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