5ieu: Difference between revisions

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== Function ==
== 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>  
[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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== Publication Abstract from PubMed ==
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.
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>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
== References ==
<references/>
<references/>

Latest revision as of 15:34, 6 March 2024

Crystal Structure of Mycobacterium Tuberculosis ATP-independent Proteasome Activator TetramerCrystal Structure of Mycobacterium Tuberculosis ATP-independent Proteasome Activator Tetramer

Structural highlights

5ieu is a 2 chain structure with sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.8Å
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]

References

  1. ↑ 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

5ieu, resolution 2.80Å

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OCA
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