3TXM

Crystal structure of Rpn6 from Drosophila melanogaster, Gd(3+) complex

Summary for 3TXM

• Entry DOI: 10.2210/pdb3txm/pdb
• Related: 3TXN
• Descriptor: 26S proteasome regulatory complex subunit p42B, GADOLINIUM ION, SULFATE ION (3 entities in total)
• Functional Keywords: 26 s proteasome, pci domain, alpha solenoid, regulatory particle, lid, hydrolase, protein binding
• Biological source: Drosophila melanogaster (Fruit fly)
• Total number of polymer chains: 1
• Total formula weight: 45038.00

Authors

Pathare, G.R.,Bracher, A. (deposition date: 2011-09-23, release date: 2011-12-14, Last modification date: 2024-02-28)

Primary citation

Pathare, G.R.,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.
The proteasomal subunit Rpn6 is a molecular clamp holding the core and regulatory subcomplexes together.
Proc.Natl.Acad.Sci.USA, 109:149-154, 2012

PubMed Abstract: Proteasomes 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 Å resolution. Rpn6 consists of an α-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.

PubMed: 22187461
DOI: 10.1073/pnas.1117648108

Experimental method

X-RAY DIFFRACTION (3 Å)