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.
Publication types
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Research Support, N.I.H., Extramural
MeSH terms
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Amino Acid Sequence
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Bacterial Proteins / chemistry*
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism
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Bacteroides / chemistry*
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Bacteroides / enzymology
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Bacteroides / genetics
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Binding Sites
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DNA Helicases / chemistry*
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DNA Helicases / genetics
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DNA Helicases / metabolism
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DNA, Bacterial / chemistry*
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DNA, Bacterial / genetics
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DNA, Bacterial / metabolism
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Models, Molecular
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Molecular Sequence Data
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Nuclear Magnetic Resonance, Biomolecular
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Protein Binding
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Protein Folding
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Protein Structure, Secondary
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Protein Structure, Tertiary
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Sequence Homology, Amino Acid
Substances
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Bacterial Proteins
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DNA, Bacterial
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Recombinant Proteins
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DNA Helicases