3txm
Crystal structure of Rpn6 from Drosophila melanogaster, Gd(3+) complexCrystal structure of Rpn6 from Drosophila melanogaster, Gd(3+) complex
Structural highlights
Function[PSD11_DROME] Component of the lid subcomplex of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. In the complex, RPN6 is required for proteasome assembly (By similarity). May act as linker between 19S regulatory subunit and the 20S proteasome core.[1] Publication Abstract from PubMedProteasomes execute the degradation of most cellular proteins. Although the 20S core particle (CP) has been studied in great detail, the structure of the 19S regulatory particle (RP), which prepares ubiquitylated substrates for degradation, has remained elusive. Here, we report the crystal structure of one of the RP subunits, Rpn6, and we describe its integration into the cryo-EM density map of the 26S holocomplex at 9.1 A resolution. Rpn6 consists of an alpha-solenoid-like fold and a proteasome COP9/signalosome eIF3 (PCI) module in a right-handed suprahelical configuration. Highly conserved surface areas of Rpn6 interact with the conserved surfaces of the Pre8 (alpha2) and Rpt6 subunits from the alpha and ATPase rings, respectively. The structure suggests that Rpn6 has a pivotal role in stabilizing the otherwise weak interaction between the CP and the RP. The proteasomal subunit Rpn6 is a molecular clamp holding the core and regulatory subcomplexes together.,Pathare GR, Nagy I, Bohn S, Unverdorben P, Hubert A, Korner R, Nickell S, Lasker K, Sali A, Tamura T, Nishioka T, Forster F, Baumeister W, Bracher A Proc Natl Acad Sci U S A. 2012 Jan 3;109(1):149-54. Epub 2011 Dec 20. PMID:22187461[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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