1QZE: HHR23a protein structure based on residual dipolar coupling data

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.
PDB ID: 1QZEDownload
MMDB ID: 25122
PDB Deposition Date: 2003/9/16
Updated in MMDB: 2003/11
Experimental Method:
solution nmr
Source Organism:
Similar Structures:
Molecular Components in 1QZE
Label Count Molecule
Protein (1 molecule)
UV Excision Repair Protein Rad23 Homolog a(Gene symbol: RAD23A)
Molecule annotation
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Citing MMDB