Structural highlights
Function
[A0R198_MYCS2] Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.[HAMAP-Rule:MF_00444]
Publication Abstract from PubMed
The ClpP protease is found in all kingdoms of life, from bacteria to humans. In general, this protease forms a homo-oligomeric complex composed of 14 identical subunits, which associates with its cognate ATPase in a symmetrical manner. Here we show that, in contrast to this general architecture, the Clp protease from Mycobacterium smegmatis (Msm) forms an asymmetric hetero-oligomeric complex ClpP1P2, which only associates with its cognate ATPase through the ClpP2 ring. Our structural and functional characterisation of this complex demonstrates that asymmetric docking of the ATPase component is controlled by both the composition of the ClpP1 hydrophobic pocket (Hp) and the presence of a unique C-terminal extension in ClpP1 that guards this Hp. Our structural analysis of (Msm)ClpP1 also revealed openings in the side-walls of the inactive tetradecamer, which may represent sites for product egress.
Molecular and structural insights into an asymmetric proteolytic complex (ClpP1P2) from Mycobacterium smegmatis.,Nagpal J, Paxman JJ, Zammit JE, Alhuwaider A, Truscott KN, Heras B, Dougan DA Sci Rep. 2019 Dec 2;9(1):18019. doi: 10.1038/s41598-019-53736-8. PMID:31792243[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Nagpal J, Paxman JJ, Zammit JE, Alhuwaider A, Truscott KN, Heras B, Dougan DA. Molecular and structural insights into an asymmetric proteolytic complex (ClpP1P2) from Mycobacterium smegmatis. Sci Rep. 2019 Dec 2;9(1):18019. doi: 10.1038/s41598-019-53736-8. PMID:31792243 doi:http://dx.doi.org/10.1038/s41598-019-53736-8
