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PDBsum entry 2zxp
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References listed in PDB file
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Key reference
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Title
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Structure of recj exonuclease defines its specificity for single-Stranded DNA.
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Authors
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T.Wakamatsu,
Y.Kitamura,
Y.Kotera,
N.Nakagawa,
S.Kuramitsu,
R.Masui.
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Ref.
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J Biol Chem, 2010,
285,
9762-9769.
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PubMed id
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Abstract
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RecJ is a single-stranded DNA (ssDNA)-specific 5'-3' exonuclease that plays an
important role in DNA repair and recombination. To elucidate how RecJ achieves
its high specificity for ssDNA, we determined the entire structures of RecJ both
in a ligand-free form and in a complex with Mn(2+) or Mg(2+) by x-ray
crystallography. The entire RecJ consists of four domains that form a molecule
with an O-like structure. One of two newly identified domains had structural
similarities to an oligonucleotide/oligosaccharide-binding (OB) fold. The OB
fold domain alone could bind to DNA, indicating that this domain is a novel
member of the OB fold superfamily. The truncated RecJ containing only the core
domain exhibited much lower affinity for the ssDNA substrate compared with
intact RecJ. These results support the hypothesis that these structural features
allow specific binding of RecJ to ssDNA. In addition, the structure of the
RecJ-Mn(2+) complex suggests that the hydrolysis reaction catalyzed by RecJ
proceeds through a two-metal ion mechanism.
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