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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.

SUBMITTER: Aramini JM

PROVIDER: S-EPMC3172673 | biostudies-literature | 2011 Oct

REPOSITORIES: biostudies-literature

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

Aramini James M JM Rossi Paolo P Fischer Markus M Xiao Rong R Acton Thomas B TB Montelione Gaetano T GT

Proteins 20110826 10

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 nucl ...[more]

PMID: 21905121

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