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5lfq

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Revision as of 07:09, 5 August 2020

Crystal Structure of the Bacterial Proteasome Activator Bpa of Mycobacterium tuberculosis (space group P3)

Structural highlights

5lfq is a 16 chain structure with sequence from Myctu. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Related:	5lfj
Gene:	bpa, Rv3780, MTCY13D12.14 (MYCTU)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5lfq"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of the Bacterial Proteasome Activator Bpa of Mycobacterium tuberculosis (space group P3)==
-<StructureSection load='5lfq' size='340' side='right' caption='[[5lfq]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
+<StructureSection load='5lfq' size='340' side='right'caption='[[5lfq]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5lfq]] is a 16 chain structure. 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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LFQ FirstGlance]. <br>
+<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>
 </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>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5lfj|5lfj]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/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>
+<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'>[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>
 == Function ==
@@ Line 23: / Line 24: @@
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
+[[Category: Myctu]]
 [[Category: Ban, N]]
 [[Category: Boehringer, D]]

5lfq

From Proteopedia

Revision as of 07:09, 5 August 2020

Crystal Structure of the Bacterial Proteasome Activator Bpa of Mycobacterium tuberculosis (space group P3)

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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