Structural basis for catalytic activation of a serine recombinase.
Structural basis for catalytic activation of a serine recombinase.
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DOI：
10.1016/j.str.2011.03.017
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发表时间：
2011-06-08
期刊：
影响因子：
5.7
通讯作者：
Rice, Phoebe A.
中科院分区：
文献类型：
--
作者：
Keenholtz, Ross A.;Rowland, Sally-J.;Boocock, Martin R.;Stark, W. Marshall;Rice, Phoebe A.
Sin resolvase is a site-specific serine recombinase that is normally controlled by a complex regulatory mechanism. A single mutation, Q115R, allows the enzyme to bypass the entire regulatory apparatus, such that no accessory proteins or DNA sites are required. Here we present a 1.86Å crystal structure of the Sin Q115R catalytic domain, in a tetrameric arrangement stabilized by an interaction between Arg115 residues on neighboring subunits. The subunits have undergone significant conformational changes from the inactive dimeric state previously reported. The structure provides a new high-resolution view of a serine recombinase active site that is apparently fully assembled, suggesting roles for the conserved active site residues. The structure also suggests how the dimer-tetramer transition is coupled to assembly of the active site. The tetramer is captured in a different rotational substate than that seen in previous hyperactive serine recombinase structures, and unbroken crossover site DNA can be readily modeled into its active sites.
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DOI：
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发表时间：
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影响因子：
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通讯作者：
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DOI：
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发表时间：
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影响因子：
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