Crystallization and preliminary X-ray diffraction analysis of human DNA primase
Crystallization and preliminary X-ray diffraction analysis of human DNA primase
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DOI：
10.1107/s2053230x13034432
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发表时间：
2014-02-01
影响因子：
0.9
通讯作者：
Tahirov, Tahir H.
中科院分区：
文献类型：
--
作者：
Baranovskiy, Andrey G.;Gu, Jianyou;Tahirov, Tahir H.
人引物酶合成RNA引物并将其转移到Pol α的活性位点，随后用dNTPs扩展。人类引物酶是两个亚基的异源二聚体：一个小的催化亚基（p49）和一个大的亚基（p58）。引物合成的起始和延伸步骤的结构细节，以及引物长度计数，尚不清楚。为了解决这些问题，人类引物酶的结构研究开始了。得到了两种类型的晶体。最佳衍射晶体属于空间群P1，其单位胞参数a = 86.2, b = 88.9, c = 94.68埃，α = 93.82, β = 96.57, γ = 111.72度，在不对称单元中含有全长p49和p59两个异源二聚体。
Human primase synthesizes RNA primers and transfers them to the active site of Pol alpha with subsequent extension with dNTPs. Human primase is a heterodimer of two subunits: a small catalytic subunit (p49) and a large subunit (p58). The structural details of the initiation and elongation steps of primer synthesis, as well as primer length counting, are not known. To address these questions, structural studies of human primase were initiated. Two types of crystals were obtained. The best diffracting crystals belonged to space group P1, with unit-cell parameters a = 86.2, b = 88.9, c = 94.68 angstrom, alpha = 93.82, beta = 96.57, gamma = 111.72 degrees, and contained two heterodimers of full-length p49 and p59 subunits in the asymmetric unit.