Structural highlights
Publication Abstract from PubMed
The 26S proteasome is an ATP-dependent protease responsible for selective degradation of polyubiquitylated proteins. Recent studies have suggested that proteasome assembly is a highly ordered multi-step process assisted by specific chaperones. Rpn14, an assembly chaperone for ATPase-ring formation, specifically recognizes the ATPase subunit Rpt6. The structure of Rpn14 at 2.0 A resolution in space group P6(4) has previously been reported, but the detailed mechanism of Rpn14 function remains unclear. Here, a new crystal structure of Rpn14 with an E384A mutation is presented in space group P2(1) at 1.6 A resolution. This high-resolution structure provides a framework for understanding proteasome assembly.
New crystal structure of the proteasome-dedicated chaperone Rpn14 at 1.6 A resolution.,Kim S, Nishide A, Saeki Y, Takagi K, Tanaka K, Kato K, Mizushima T Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 May 1;68(Pt 5):517-21., doi: 10.1107/S1744309112011359. Epub 2012 Apr 20. PMID:22691779[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kim S, Nishide A, Saeki Y, Takagi K, Tanaka K, Kato K, Mizushima T. New crystal structure of the proteasome-dedicated chaperone Rpn14 at 1.6 A resolution. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 May 1;68(Pt 5):517-21., doi: 10.1107/S1744309112011359. Epub 2012 Apr 20. PMID:22691779 doi:10.1107/S1744309112011359
