Crystal structure of the transcriptional activator HlyU from Vibrio vulnificus CMCP6

FEBS Lett. 2010 Mar 19;584(6):1097-102. doi: 10.1016/j.febslet.2010.02.052. Epub 2010 Feb 21.

Abstract

HlyU is a transcription factor of the ArsR/SmtB family and activates the expression of the pathogenic Vibrio vulnificus RTX toxin. In contrast to the other metal-responding ArsR/SmtB proteins, HlyU does not sense metal ions. To provide its structural information, we elucidated the crystal structure of HlyU from V. vulnificus CMCP6 (HlyU_Vv). The monomeric HlyU_Vv architecture of five alpha-helices and two beta-strands, some of which constitute a typical DNA-binding winged helix-turn-helix (wHTH) motif, is very similar to that of other transcription regulators. Nonetheless, the homo-dimeric HlyU_Vv structure shows several different, three-dimensional features in the spatial position and the detailed dimeric interaction, which were not observed in the modeling study based on the same protein family and sequence similarity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Crystallography, X-Ray
  • DNA, Bacterial / metabolism
  • Hemolysin Factors / chemistry*
  • Hemolysin Factors / metabolism
  • Metals, Heavy / metabolism
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Binding
  • Protein Conformation
  • Protein Multimerization
  • Sequence Homology, Amino Acid
  • Trans-Activators / chemistry
  • Trans-Activators / metabolism
  • Vibrio vulnificus* / genetics
  • Vibrio vulnificus* / metabolism

Substances

  • DNA, Bacterial
  • Metals, Heavy
  • Trans-Activators