title: Solution NMR structure of VF0530 from Vibrio fischeri reveals a nucleic acid-binding function.
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.
authors: Department of Molecular Biology and Biochemistry, Rutgers, The State University of New Jersey, Piscataway, New Jersey 08854, USA. jma@cabm.rutgers.edu
authors: James M
authors: JM
authors: Aramini
authors: Paolo
authors: P
authors: Rossi
authors: Markus
authors: M
authors: Fischer
authors: Rong
authors: R
authors: Xiao
authors: Thomas B
authors: TB
authors: Acton
authors: Gaetano T
authors: GT
authors: Montelione
mesh_terms: D048908:Aliivibrio fischeri / Q000378:metabolism*; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D009696:Nucleic Acids / Q000737:chemistry* / Q000378:metabolism*; D011485:Protein Binding; D017433:Protein Structure, Secondary
chemical_list: D001426:Bacterial Proteins; D009696:Nucleic Acids