4ADY

Crystal structure of 26S proteasome subunit Rpn2

Summary for 4ADY

• Entry DOI: 10.2210/pdb4ady/pdb
• Descriptor: 26S PROTEASOME REGULATORY SUBUNIT RPN2 (2 entities in total)
• Functional Keywords: protein binding, rpn1, pc repeat
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• Total number of polymer chains: 2
• Total formula weight: 214699.81

Authors

Kulkarni, K.,He, J.,Da Fonseca, P.C.A.,Krutauz, D.,Glickman, M.H.,Barford, D.,Morris, E.P. (deposition date: 2012-01-04, release date: 2012-03-14, Last modification date: 2024-10-23)

Primary citation

He, J.,Kulkarni, K.,Da Fonseca, P.C.A.,Krutauz, D.,Glickman, M.H.,Barford, D.,Morris, E.P.
The Structure of the 26S Proteasome Subunit Rpn2 Reveals its Pc Repeat Domain as a Closed Toroid of Two Concentric Alpha-Helical Rings
Structure, 20:513-, 2012

PubMed Abstract: The 26S proteasome proteolyses ubiquitylated proteins and is assembled from a 20S proteolytic core and two 19S regulatory particles (19S-RP). The 19S-RP scaffolding subunits Rpn1 and Rpn2 function to engage ubiquitin receptors. Rpn1 and Rpn2 are characterized by eleven tandem copies of a 35-40 amino acid repeat motif termed the proteasome/cyclosome (PC) repeat. Here, we reveal that the eleven PC repeats of Rpn2 form a closed toroidal structure incorporating two concentric rings of α helices encircling two axial α helices. A rod-like N-terminal domain consisting of 17 stacked α helices and a globular C-terminal domain emerge from one face of the toroid. Rpn13, an ubiquitin receptor, binds to the C-terminal 20 residues of Rpn2. Rpn1 adopts a similar conformation to Rpn2 but differs in the orientation of its rod-like N-terminal domain. These findings have implications for understanding how 19S-RPs recognize, unfold, and deliver ubiquitylated substrates to the 20S core.

PubMed: 22405010
DOI: 10.1016/J.STR.2011.12.015

Experimental method

X-RAY DIFFRACTION (2.7 Å)