The solution structure of the ZnF UBP domain of USP33/VDU1.
USP33/VDU1 is a deubiquitinating enzyme that binds to the von Hippel-Lindau tumor suppressor protein. It also regulates thyroid hormone activation by deubiquitinating type 2 iodothyronine deiodinase. USP33/VDU1 contains a ZF UBP domain, a protein module found in many proteins in the ubiquitin-proteasome system. Several ZF UBP domains have been shown to bind ubiquitin, and a structure of a complex of the ZF UBP domain of isoT/USP5 and ubiquitin is available. In the present work, the solution structure of the ZF UBP domain of USP33/VDU1 has been determined by NMR spectroscopy. The structure differs from that of the USP5 domain, which contains only one of the three Zn ions present in the USP33/VDU1 structure. The USP33/VDU1 ZnF UBP domain does not bind to ubiquitin.
Allen
Mark D
MD
Medical Research Council, The MRC Centre for Protein Engineering, Cambridge CB2 2QH, United Kingdom.
Bycroft
Mark
M
D000595:Amino Acid Sequence; D017124:Conserved Sequence; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid; D013059:Spectrum Analysis, Raman; D025801:Ubiquitin / Q000737:chemistry* / Q000378:metabolism*; D043222:Ubiquitin Thiolesterase / Q000737:chemistry*; D016335:Zinc Fingers
D025801:Ubiquitin; C449799:USP33 protein, human; D043222:Ubiquitin Thiolesterase