Structural highlights
Function
[ESPG5_MYCTU] Specific chaperone for cognate PE/PPE proteins. Plays an important role in preventing aggregation of PE/PPE dimers.[1] [PPE15_MYCTU] May play a critical role in the homeostasis of triacylglycerol-containing lipid droplets in M.tuberculosis and influence the entry of the pathogen into a dormant state.[2]
References
- ↑ Korotkova N, Freire D, Phan TH, Ummels R, Creekmore CC, Evans TJ, Wilmanns M, Bitter W, Parret AH, Houben EN, Korotkov KV. Structure of the Mycobacterium tuberculosis type VII secretion system chaperone EspG in complex with PE25-PPE41 dimer. Mol Microbiol. 2014 Aug 26. doi: 10.1111/mmi.12770. PMID:25155747 doi:http://dx.doi.org/10.1111/mmi.12770
- ↑ Daniel J, Kapoor N, Sirakova T, Sinha R, Kolattukudy P. The perilipin-like PPE15 protein in Mycobacterium tuberculosis is required for triacylglycerol accumulation under dormancy-inducing conditions. Mol Microbiol. 2016 Sep;101(5):784-94. doi: 10.1111/mmi.13422. Epub 2016 Jun 21. PMID:27325376 doi:http://dx.doi.org/10.1111/mmi.13422
