2N3T

Solution structure of the Rpn1 substrate receptor site toroid 1 (T1)

Summary for 2N3T

• Entry DOI: 10.2210/pdb2n3t/pdb
• Related: 2N3U 2N3V 2N3W
• NMR Information: BMRB: 25657
• Descriptor: 26S proteasome regulatory subunit RPN1 (1 entity in total)
• Functional Keywords: protein binding
• Biological source: Saccharomyces cerevisiae (Baker's yeast)
• Total number of polymer chains: 1
• Total formula weight: 13636.59

Authors

Chen, X.,Walters, K.J. (deposition date: 2015-06-10, release date: 2016-02-24, Last modification date: 2024-05-15)

Primary citation

Shi, Y.,Chen, X.,Elsasser, S.,Stocks, B.B.,Tian, G.,Lee, B.H.,Shi, Y.,Zhang, N.,de Poot, S.A.,Tuebing, F.,Sun, S.,Vannoy, J.,Tarasov, S.G.,Engen, J.R.,Finley, D.,Walters, K.J.
Rpn1 provides adjacent receptor sites for substrate binding and deubiquitination by the proteasome.
Science, 351:-, 2016

PubMed Abstract: Hundreds of pathways for degradation converge at ubiquitin recognition by a proteasome. Here, we found that the five known proteasomal ubiquitin receptors in yeast are collectively nonessential for ubiquitin recognition and identified a sixth receptor, Rpn1. A site ( T1: ) in the Rpn1 toroid recognized ubiquitin and ubiquitin-like ( UBL: ) domains of substrate shuttling factors. T1 structures with monoubiquitin or lysine 48 diubiquitin show three neighboring outer helices engaging two ubiquitins. T1 contributes a distinct substrate-binding pathway with preference for lysine 48-linked chains. Proximal to T1 within the Rpn1 toroid is a second UBL-binding site ( T2: ) that assists in ubiquitin chain disassembly, by binding the UBL of deubiquitinating enzyme Ubp6. Thus, a two-site recognition domain intrinsic to the proteasome uses distinct ubiquitin-fold ligands to assemble substrates, shuttling factors, and a deubiquitinating enzyme.

PubMed: 26912900
DOI: 10.1126/science.aad9421

Experimental method

SOLUTION NMR