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Protein Science (2007), 16:2072-2075. Published by Cold Spring Harbor Laboratory Press. Copyright © 2007 The Protein Society
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PROTEIN STRUCTURE REPORT

The solution structure of the ZnF UBP domain of USP33/VDU1

Mark D. Allen and Mark Bycroft

Medical Research Council, The MRC Centre for Protein Engineering, Cambridge CB2 2QH, United Kingdom

(RECEIVED April 26, 2007; FINAL REVISION May 28, 2007; ACCEPTED May 29, 2007)

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.

Keywords: VHL; deubiquitination; HDAC6; IMP


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