Structural highlights
Function
DNABP_ALIF1 Binds double-stranded DNA (dsDNA).[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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; (c) 2011 Wiley-Liss, Inc.
Solution NMR structure of VF0530 from Vibrio fischeri reveals a nucleic acid-binding function.,Aramini JM, Rossi P, Fischer M, Xiao R, Acton TB, Montelione GT Proteins. 2011 Oct;79(10):2988-91. doi: 10.1002/prot.23121. Epub 2011 Aug, 26. PMID:21905121[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Aramini JM, Rossi P, Fischer M, Xiao R, Acton TB, Montelione GT. Solution NMR structure of VF0530 from Vibrio fischeri reveals a nucleic acid-binding function. Proteins. 2011 Oct;79(10):2988-91. doi: 10.1002/prot.23121. Epub 2011 Aug, 26. PMID:21905121 doi:10.1002/prot.23121
- ↑ Aramini JM, Rossi P, Fischer M, Xiao R, Acton TB, Montelione GT. Solution NMR structure of VF0530 from Vibrio fischeri reveals a nucleic acid-binding function. Proteins. 2011 Oct;79(10):2988-91. doi: 10.1002/prot.23121. Epub 2011 Aug, 26. PMID:21905121 doi:10.1002/prot.23121