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Solution NMR structures reveal unique homodimer formation by a winged helix-turn-helix motif and provide first structures for protein domain family PF10771

  • Published:
Journal of Structural and Functional Genomics

An Erratum to this article was published on 06 March 2012

Abstract

High-quality NMR structures of the homo-dimeric proteins Bvu3908 (69-residues in monomeric unit) from Bacteroides vulgatus and Bt2368 (74-residues) from Bacteroides thetaiotaomicron reveal the presence of winged helix-turn-helix (wHTH) motifs mediating tight complex formation. Such homo-dimer formation by winged HTH motifs is otherwise found only in two DNA-binding proteins with known structure: the C-terminal wHTH domain of transcriptional activator FadR from E. coli and protein TubR from B. thurigensis, which is involved in plasmid DNA segregation. However, the relative orientation of the wHTH motifs is different and residues involved in DNA-binding are not conserved in Bvu3908 and Bt2368. Hence, the proteins of the present study are not very likely to bind DNA, but are likely to exhibit a function that has thus far not been ascribed to homo-dimers formed by winged HTH motifs. The structures of Bvu3908 and Bt2368 are the first atomic resolution structures for PFAM family PF10771, a family of unknown function (DUF2582) currently containing 128 members.

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Fig. 1

Abbreviations

DSS:

4,4-Dimethyl-4-silapentane-1-sulfonate sodium salt

DTT:

Dithiothreitol

HTH:

Helix-turn-helix

MES:

2-(N-Morpholino)ethanesulfonic acid

NESG:

Northeast Structural Genomics Consortium

NOE:

Nuclear Overhauser effect

PDB:

Protein Data Bank

RDC:

Residual dipolar coupling

RMSD:

Root mean square deviation

wHTH:

Winged helix-turn-helix

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Acknowledgments

We thank D. Wang, C. Ciccosanti, K. Hamilton and S. Bhattacharya for helpful discussions and technical support. This work was supported by the National Institutes of Health, grant number: U54 GM094597 (T.S. and G.T.M.). While data acquisition was in progress, Prof. T. Szyperski was a member of the New York Structural Biology Center. The Center is a STAR center supported by the New York State Office of Science, Technology, and Academic Research.

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Authors and Affiliations

  1. Department of Chemistry, The State University of New York at Buffalo, and Northeast Structural Genomics Consortium, Buffalo, NY, 14260, USA

    Alexander Eletsky & Thomas Szyperski

  2. Department of Biochemistry and Molecular Biophysics, Howard Hughes Medical Institute, Center for Computational Biology and Bioinformatics, Columbia University, New York, NY, 10032, USA

    Donald Petrey, Qiangfeng Cliff Zhang & Barry Honig

  3. Complex Carbohydrate Research Center, University of Georgia, and Northeast Structural Genomics Consortium, Athens, GA, 30602, USA

    Hsiau-Wei Lee & James H. Prestegard

  4. Department of Molecular Biology and Biochemistry, Center of Advanced Biotechnology and Medicine, Rutgers, The State University of New Jersey, Piscataway, NJ, 08854, USA

    Thomas B. Acton, Rong Xiao, John K. Everett & Gaetano T. Montelione

  5. Department of Biochemistry, Robert Wood Johnson Medical School, UMDNJ, and Northeast Structural Genomics Consortium, Piscataway, NJ, 08854, USA

    Thomas B. Acton, Rong Xiao, John K. Everett & Gaetano T. Montelione

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  1. Alexander Eletsky
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Additional information

An erratum to this article can be found at http://dx.doi.org/10.1007/s10969-012-9132-8.

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Eletsky, A., Petrey, D., Zhang, Q.C. et al. Solution NMR structures reveal unique homodimer formation by a winged helix-turn-helix motif and provide first structures for protein domain family PF10771. J Struct Funct Genomics 13, 1–7 (2012). https://doi.org/10.1007/s10969-011-9121-3

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