5ieu

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

↑ 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

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OCA

[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

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