1OQY

Structure of the DNA repair protein hHR23a

Summary for 1OQY

• Entry DOI: 10.2210/pdb1oqy/pdb
• Related: 1qze
• Descriptor: UV excision repair protein RAD23 homolog A (1 entity in total)
• Functional Keywords: dna repair, proteasome-mediated degradation, protein-protein interaction, replication
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: P54725
• Total number of polymer chains: 1
• Total formula weight: 40009.32

Authors

Walters, K.J.,Lech, P.J.,Goh, A.M.,Wang, Q.,Howley, P.M. (deposition date: 2003-03-11, release date: 2003-10-21, Last modification date: 2024-05-22)

Primary citation

Walters, K.J.,Lech, P.J.,Goh, A.M.,Wang, Q.,Howley, P.M.
DNA-repair protein hHR23a alters its protein structure upon binding proteasomal subunit S5a
Proc.Natl.Acad.Sci.USA, 100:12694-12699, 2003

PubMed Abstract: The Rad23 family of proteins, including the human homologs hHR23a and hHR23b, stimulates nucleotide excision repair and has been shown to provide a novel link between proteasome-mediated protein degradation and DNA repair. In this work, we illustrate how the proteasomal subunit S5a regulates hHR23a protein structure. By using NMR spectroscopy, we have elucidated the structure and dynamic properties of the 40-kDa hHR23a protein and show it to contain four structured domains connected by flexible linker regions. In addition, we reveal that these domains interact in an intramolecular fashion, and by using residual dipolar coupling data in combination with chemical shift perturbation analysis, we present the hHR23a structure. By itself, hHR23a adopts a closed conformation defined by the interaction of an N-terminal ubiquitin-like domain with two ubiquitin-associated domains. Interestingly, binding of the proteasomal subunit S5a disrupts the hHR23a interdomain interactions and thereby causes it to adopt an opened conformation.

PubMed: 14557549
DOI: 10.1073/pnas.1634989100

Experimental method

SOLUTION NMR