3whl
From Proteopedia
Revision as of 07:37, 16 April 2014
Contents |
Crystal structure of Nas2 N-terminal domain complexed with PAN-Rpt5C chimera
Template:ABSTRACT PUBMED 24685148
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). [PSMD9_YEAST] Acts as a chaperone during the assembly of the 26S proteasome, specifically of the base subcomplex of the 19S regulatory complex (RC). During the base subcomplex assembly is part of a NAS2:RPT4:RPT5 module; NAS2 is released during the further base assembly process.
About this Structure
3whl is a 8 chain structure with sequence from Baker's yeast and 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:http://dx.doi.org/10.1016/j.str.2014.02.014
Categories: Baker's yeast | Pyrfu | Hiromoto, T. | Kato, K. | Mizushima, T. | Saeki, Y. | Satoh, T. | Tanaka, K. | Uekusa, Y. | Wang, Y H. | Yagi, H. | Yagi-Utsumi, M. | Yoshihara, H. | Atp binding | Four-helix bundle | Hydrolase-chaperone complex | Proteasome assembly chaperone | Proteasome atpase subunit