Solution structure of the RNA polymerase subunit RPB5 from Methanobacterium thermoautotrophicum.

Solution structure of the RNA polymerase subunit RPB5 from Methanobacterium thermoautotrophicum.
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来自热自养甲烷杆菌的 RNA 聚合酶亚基 RPB5 的溶液结构。

DOI:
10.1073/pnas.97.12.6311
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发表时间:
2000
影响因子:
11.1
通讯作者:
C. Arrowsmith
C. Arrowsmith
中科院分区:
综合性期刊1区
文献类型:
--
作者:
A. Yee;V. Booth;A. Dharamsi;A. Engel;A. Edwards;C. Arrowsmith

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RPB5是真核生物和古细菌RNA聚合酶的重要亚基。它是真核生物中转录激活蛋白的靶点,但其相互作用机制尚不清楚。我们已经确定了嗜热源生甲烷菌(Methanobacterium thermoautotrophicum) RPB5亚基的溶液结构。MtRBP5包含一个四链β -片平台,支持两个α -螺旋,每个α -片的两侧各有一个,从而形成一个整体的蘑菇形状,在结构数据库中似乎没有任何结构同源物。带电表面残基的位置和守恒表明了与其他蛋白质相互作用的可能模式,以及该蛋白质热稳定性的基本原理。
RPB5 is an essential subunit of eukaryotic and archaeal RNA polymerases. It is a proposed target for transcription activator proteins in eukaryotes, but the mechanism of interaction is not known. We have determined the solution structure of the RPB5 subunit from the thermophilic archeon, Methanobacterium thermoautotrophicum. MtRBP5 contains a four-stranded beta-sheet platform supporting two alpha-helices, one on each side of the beta-sheet, resulting in an overall mushroom shape that does not appear to have any structural homologues in the structural database. The position and conservation of charged surface residues suggests possible modes of interaction with other proteins, as well as a rationale for the thermal stability of this protein.
DOI: 10.1073/pnas.95.26.15281
发表时间: 1998-12-22
影响因子: 11.1
作者:
Miyao, T;Woychik, NA
通讯作者: Woychik, NA
DOI: 10.1016/s0021-9258(18)52403-0
发表时间: 1991-01
期刊: The Journal of biological chemistry
影响因子: --
作者:
Aled M. Edwards;C. Kane;Richard A. Young;R. Kornberg
通讯作者: Aled M. Edwards;C. Kane;Richard A. Young;R. Kornberg