Crystallization and preliminary X-ray diffraction studies of the ubiquitin-like (UbL) domain of the human homologue A of Rad23 (hHR23A) protein.
Human homologue A of Rad23 (hHR23A) plays dual roles in DNA repair as well as serving as a shuttle vehicle targeting polyubiquitinated proteins for degradation. Its N-terminal ubiquitin-like (UbL) domain interacts with the 19S proteasomal cap and provides the docking mechanism for protein delivery. Pyramidal crystals of the UbL domain of hHR23A were obtained by the hanging-drop vapour-diffusion method with ammonium sulfate as the crystallizing agent. The crystals diffracted to beyond 2 A resolution and belonged to the hexagonal space group P6(5)22, with unit-cell parameters a = b = 78.48, c = 63.57 A. The structure was solved by molecular replacement using the UbL domain of yeast Dsk2 as the search model.
Chen
Yu Wai
YW
Randall Division of Cell and Molecular Biophysics, King's College London, London, England. yu-wai.chen@kcl.ac.uk
Tajima
Toshitaka
T
Rees
Martin
M
Garcia-Maya
Mitla
M
D003460:Crystallization; D018360:Crystallography, X-Ray; D045643:DNA Repair Enzymes / Q000737:chemistry*; D004268:DNA-Binding Proteins / Q000737:chemistry*; D006801:Humans; D017434:Protein Structure, Tertiary; D025801:Ubiquitin / Q000737:chemistry*; D014961:X-Ray Diffraction
D004268:DNA-Binding Proteins; D025801:Ubiquitin; C086985:RAD23A protein, human; D045643:DNA Repair Enzymes