3whk | pdb_00003whk
Crystal structure of PAN-Rpt5C chimera
Function
[PAN_PYRFU] ATPase which is responsible for recognizing, binding, unfolding and translocation of substrate proteins into the archaeal 20S proteasome core particle. Is essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. Unfolding activity requires energy from ATP hydrolysis, whereas ATP binding alone promotes ATPase-20S proteasome association which triggers gate opening, and supports translocation of unfolded substrates (By similarity).
About this Structure
3whk is a 8 chain structure with sequence from Pyrfu. Full crystallographic information is available from OCA.
Reference
- Satoh T, Saeki Y, Hiromoto T, Wang YH, Uekusa Y, Yagi H, Yoshihara H, Yagi-Utsumi M, Mizushima T, Tanaka K, Kato K. Structural Basis for Proteasome Formation Controlled by an Assembly Chaperone Nas2. Structure. 2014 Mar 25. pii: S0969-2126(14)00070-7. doi:, 10.1016/j.str.2014.02.014. PMID:24685148 doi:https://dx.doi.org/10.1016/j.str.2014.02.014
