Abstract
A high-quality NMR structure of the helicase associated (HA) domain comprising residues 627–691 of the 753-residue protein BVU_0683 from Bacteroides vulgatus exhibits an all α-helical fold. The structure presented here is the first representative for the large protein domain family PF03457 (currently 742 members) of HA domains. Comparison with structurally similar proteins supports the hypothesis that HA domains bind to DNA and that binding specificity varies greatly within the family of HA domains constituting PF03457.
Abbreviations
- DNA:
-
Deoxyribonucleic acid
- DSS:
-
4,4-dimethyl-4-silapentane-1-sulfonate sodium salt
- DTT:
-
Dithiothreitol
- HA:
-
Helicase associated
- ISW:
-
Imitation switch
- MES:
-
2-(N-morpholino)ethanesulfonic acid
- NESG:
-
Northeast structural genomics consortium
- NOE:
-
Nuclear overhauser effect
- PDB:
-
Protein data bank
- RMSD:
-
Root mean square deviation
- SANT:
-
SWI3, ADA2, N-CoR, and TFIIIB
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Acknowledgments
We thank R. Belote, C. Ciccosanti, K. Hamilton, and G.V.T. Swapna 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.).
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Mills, J.L., Acton, T.B., Xiao, R. et al. Solution NMR structure of the helicase associated domain BVU_0683(627–691) from Bacteroides vulgatus provides first structural coverage for protein domain family PF03457 and indicates domain binding to DNA. J Struct Funct Genomics 14, 19–24 (2013). https://doi.org/10.1007/s10969-012-9148-0
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DOI: https://doi.org/10.1007/s10969-012-9148-0