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Proteins. 2011 Oct;79(10):2988-91. doi: 10.1002/prot.23121. Epub 2011 Aug 26.

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

Author information

1
Department of Molecular Biology and Biochemistry, Rutgers, The State University of New Jersey, Piscataway, New Jersey 08854, USA. jma@cabm.rutgers.edu

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.

PMID:
21905121
PMCID:
PMC3172673
DOI:
10.1002/prot.23121
[Indexed for MEDLINE]
Free PMC Article

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