5ieu

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==Crystal Structure of Mycobacterium Tuberculosis ATP-independent Proteasome Activator Tetramer==
==Crystal Structure of Mycobacterium Tuberculosis ATP-independent Proteasome Activator Tetramer==
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<StructureSection load='5ieu' size='340' side='right' caption='[[5ieu]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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<StructureSection load='5ieu' size='340' side='right'caption='[[5ieu]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5ieu]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IEU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5IEU FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5ieu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IEU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IEU FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5iet|5iet]]</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
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<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=5ieu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ieu OCA], [http://pdbe.org/5ieu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ieu RCSB], [http://www.ebi.ac.uk/pdbsum/5ieu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ieu ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ieu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ieu OCA], [https://pdbe.org/5ieu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ieu RCSB], [https://www.ebi.ac.uk/pdbsum/5ieu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ieu ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[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>
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The human pathogenMycobacterium tuberculosis(Mtb) requires a proteasome system to cause lethal infections in mice. We recently found that proteasome accessory factor E (PafE, Rv3780) activates proteolysis by theMtbproteasome independently of adenosine triphosphate (ATP). Moreover, PafE contributes to the heat-shock response and virulence ofMtb Here, we show that PafE subunits formed four-helix bundles similar to those of the eukaryotic ATP-independent proteasome activator subunits of PA26 and PA28. However, unlike any other known proteasome activator, PafE formed dodecamers with 12-fold symmetry, which required a glycine-XXX-glycine-XXX-glycine motif that is not found in previously described activators. Intriguingly, the truncation of the PafE carboxyl-terminus resulted in the robust binding of PafE rings to native proteasome core particles and substantially increased proteasomal activity, suggesting that the extended carboxyl-terminus of this cofactor confers suboptimal binding to the proteasome core particle. Collectively, our data show that proteasomal activation is not limited to hexameric ATPases in bacteria.
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Structural analysis of the dodecameric proteasome activator PafE in Mycobacterium tuberculosis.,Bai L, Hu K, Wang T, Jastrab JM, Darwin KH, Li H Proc Natl Acad Sci U S A. 2016 Mar 21. pii: 201512094. PMID:27001842<ref>PMID:27001842</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5ieu" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bai, L]]
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[[Category: Large Structures]]
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[[Category: Darwin, K H]]
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[[Category: Mycobacterium tuberculosis]]
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[[Category: Hu, K]]
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[[Category: Bai L]]
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[[Category: Jastrab, J B]]
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[[Category: Darwin KH]]
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[[Category: Li, H]]
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[[Category: Hu K]]
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[[Category: Wang, T]]
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[[Category: Jastrab JB]]
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[[Category: Activator]]
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[[Category: Li H]]
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[[Category: Gene regulation]]
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[[Category: Wang T]]

Current revision

Crystal Structure of Mycobacterium Tuberculosis ATP-independent Proteasome Activator Tetramer

PDB ID 5ieu

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