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

✍ Scribed by James M. Aramini; Paolo Rossi; Markus Fischer; Rong Xiao; Thomas B. Acton; Gaetano T. Montelione

• Publisher: John Wiley and Sons
• Year: 2011
• Tongue: English
• Weight: 997 KB
• Volume: 79
• Category: Article
• ISSN: 0887-3585
• DOI: 10.1002/prot.23121

✦ Synopsis

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. Proteins 2011; © 2011 Wiley‐Liss, Inc.