Publication Abstract from PubMed
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. Proteins 2011; (c) 2011 Wiley-Liss, Inc.
Solution NMR structure of VF0530 from Vibrio fischeri reveals a nucleic acid-binding function.,Aramini JM, Rossi P, Fischer M, Xiao R, Acton TB, Montelione GT Proteins. 2011 Oct;79(10):2988-91. doi: 10.1002/prot.23121. Epub 2011 Aug, 26. PMID:21905121[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
