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Old 09-10-2011, 06:51 PM
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Default Solution NMR structure of VF0530 from Vibrio fischeri reveals a nucleic acid-binding function.

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

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

Proteins. 2011 Oct;79(10):2988-91

Authors: Aramini JM, Rossi P, Fischer M, Xiao R, Acton TB, Montelione GT

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.


PMID: 21905121 [PubMed - in process]



Source: PubMed
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