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

Protein Sci. 2007 Sep;16(9):2072-5. doi: 10.1110/ps.072967807.

Abstract

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.

MeSH terms

  • Amino Acid Sequence
  • Conserved Sequence
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Nuclear Magnetic Resonance, Biomolecular
  • Protein Conformation
  • Protein Structure, Tertiary
  • Sequence Homology, Amino Acid
  • Spectrum Analysis, Raman
  • Ubiquitin / chemistry*
  • Ubiquitin / metabolism*
  • Ubiquitin Thiolesterase / chemistry*
  • Zinc Fingers*

Substances

  • Ubiquitin
  • USP33 protein, human
  • Ubiquitin Thiolesterase