View source for 5lfj


==Crystal Structure of the Bacterial Proteasome Activator Bpa of Mycobacterium tuberculosis==
<StructureSection load='5lfj' size='340' side='right'caption='[[5lfj]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5lfj]] is a 4 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=5LFJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LFJ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</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=5lfj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lfj OCA], [https://pdbe.org/5lfj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lfj RCSB], [https://www.ebi.ac.uk/pdbsum/5lfj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lfj ProSAT]</span></td></tr>
</table>
== Function ==
[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;">
== 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<ref>PMID:27839949</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5lfj" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mycobacterium tuberculosis H37Rv]]
[[Category: Ban N]]
[[Category: Boehringer D]]
[[Category: Bolten M]]
[[Category: Delley CL]]
[[Category: Leibundgut M]]
[[Category: Weber-Ban E]]