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

Department of Molecular Biology and Biochemistry, Rutgers, The State University of New Jersey, Piscataway, New Jersey 08854, USA. jma@cabm.rutgers.edu

Proteins 2011 Oct

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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. Copyright © 2011 Wiley-Liss, Inc.

Citation

James M Aramini, Paolo Rossi, Markus Fischer, Rong Xiao, Thomas B Acton, Gaetano T Montelione. Solution NMR structure of VF0530 from Vibrio fischeri reveals a nucleic acid-binding function. Proteins. 2011 Oct;79(10):2988-91