3vl1 | pdb_00003vl1
Crystal structure of yeast Rpn14
Structural highlights
Function[RPN14_YEAST] Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. Is not a genuine component of the 26S proteasome, but an auxiliary factor that interacts with the proteasomal ATPase of 19S regulatory particle (RP). Acts as a chaperone which regulates the highly structured assembly of the 19S regulatory particle. Involved in the substrate specificity of the 26S proteasome and is especially involved in the degradation of ubiquitinated GCN4. May contribute to the stability of the 26S proteasome in some stress conditions.[1] [2] [3] [4] Publication Abstract from PubMedThe 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[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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