1P9D

High-resolution structure of the complex of HHR23A ubiquitin-like domain and the C-terminal ubiquitin-interacting motif of proteasome subunit S5a

Summary for 1P9D

• Entry DOI: 10.2210/pdb1p9d/pdb
• Related: 1P98 1P9C
• Descriptor: 26S proteasome non-ATPase regulatory subunit 4, UV excision repair protein RAD23 homolog A (2 entities in total)
• Functional Keywords: protein-peptide complex, replication
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: P54725
• Total number of polymer chains: 2
• Total formula weight: 13869.88

Authors

Mueller, T.D.,Feigon, J. (deposition date: 2003-05-10, release date: 2003-10-07, Last modification date: 2024-05-22)

Primary citation

Mueller, T.D.,Feigon, J.
Structural determinants for the binding of ubiquitin-like domains to the proteasome.
Embo J., 22:4634-4645, 2003

PubMed Abstract: HHR23A, a protein implicated in nucleotide excision repair, belongs to a class of proteins containing both a ubiquitin-like (Ubl) domain and one or more ubiquitin-associated (UBA) domains, suggesting a role in the ubiquitin-proteasome pathway as well. The Ubl domain binds with high affinity to the second ubiquitin-interacting motif (UIM) of the S5a subunit of the proteasome. Here we present the solution structures of the HHR23A Ubl domain, the second UIM of S5a (UIM-2), and the Ubl:S5a-UIM-2 complex. The HHR23A Ubl domain is structurally similar to ubiquitin. The S5a UIM forms an alpha-helix with an unexpected hairpin loop that contributes to the binding interface with Ubl. The molecular determinants of the Ubl-proteasome interaction are revealed by analysis of the structures, chemical shift mapping, mutant binding studies and sequence conservation.

PubMed: 12970176
DOI: 10.1093/emboj/cdg467

Experimental method

SOLUTION NMR