Solution NMR structure of VF0530 from Vibrio fischeri reveals a nucleic acid-binding function

James M. Aramini, Paolo Rossi, Markus Fischer, Rong Xiao, Thomas B. Acton, Gaetano T. Montelione

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

Abstract

Protein domain family PF09905 (DUF2132) is a family of small domains of unknown function that are conserved in a wide range of bacteria. Here we describe the solution NMR structure of the 80-residue VF0530 protein from Vibrio fischeri, the first structural representative from this protein domain family. We demonstrate that the structure of VF0530 adopts a unique four-helix motif that shows some similarity to the C-terminal double-stranded DNA (dsDNA) binding domain of RecA, as well as other nucleic acid binding domains. Moreover, gel shift binding data indicate a potential dsDNA binding role for VF0530.

Original languageEnglish (US)
Pages (from-to)2988-2991
Number of pages4
JournalProteins: Structure, Function and Bioinformatics
Volume79
Issue number10
DOIs
StatePublished - Oct 2011

Keywords

  • DUF2132
  • Nucleic acid-binding domain
  • PF09905
  • Structural genomics

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