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PDBsum entry 2mh2
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DNA binding protein
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PDB id
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2mh2
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References listed in PDB file
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Key reference
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Title
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Solution structure and DNA-Binding properties of the winged helix domain of the meiotic recombination hop2 protein.
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Authors
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H.Moktan,
M.F.Guiraldelli,
C.A.Eyster,
W.Zhao,
C.Y.Lee,
T.Mather,
R.D.Camerini-Otero,
P.Sung,
D.H.Zhou,
R.J.Pezza.
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Ref.
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J Biol Chem, 2014,
289,
14682-14691.
[DOI no: ]
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PubMed id
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Abstract
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The HOP2 protein is required for efficient double-strand break repair which
ensures the proper synapsis of homologous chromosomes and normal meiotic
progression. We previously showed that in vitro HOP2 shows two distinctive
activities: when it is incorporated into a HOP2-MND1 heterodimer, it stimulates
DMC1 and RAD51 recombination activities, and the purified HOP2 alone is
proficient in promoting strand invasion. The structural and biochemical basis of
HOP2 action in recombination are poorly understood; therefore, they are the
focus of this work. Herein, we present the solution structure of the
amino-terminal portion of mouse HOP2, which contains a typical winged helix
DNA-binding domain. Together with NMR spectral changes in the presence of
double-stranded DNA, protein docking on DNA, and mutation analysis to identify
the amino acids involved in DNA coordination, our results on the
three-dimensional structure of HOP2 provide key information on the fundamental
structural and biochemical requirements directing the interaction of HOP2 with
DNA. These results, in combination with mutational experiments showing the role
of a coiled-coil structural feature involved in HOP2 self-association, allow us
to explain important aspects of the function of HOP2 in recombination.
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