Structure of the stand-alone RAM-domain protein from Thermus thermophilus HB8.
Structure of the stand-alone RAM-domain protein from Thermus thermophilus HB8.
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来自嗜热栖热菌 HB8 的独立 RAM 结构域蛋白的结构。
DOI：
10.1107/s1744309106031150
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发表时间：
2006
期刊：
影响因子：
--
通讯作者：
S. Yokoyama
中科院分区：
文献类型：
--
作者：
N. Nakano;N. Okazaki;S. Satoh;K. Takio;S. Kuramitsu;A. Shinkai;S. Yokoyama
来自嗜热栖热菌 HB8 (TTHA0845) 的独立 RAM（氨基酸代谢调节）结构域蛋白 SraA 在锌离子存在下结晶。 X 射线晶体结构采用多波长反常色散技术测定，并以 2.4 A 分辨率进行细化，最终 R 因子为 25.0%。单体结构是βαββαβ折叠，主要通过反平行β-折叠之间的相互作用形成二聚体。此外，五个SraA二聚体形成一个外径和内径分别为70和20 A的环。与其他独立 RAM 结构域蛋白和 Lrp/AsnC 家族蛋白 C 端 RAM 结构域的八聚体和十二聚体结构相比，这种十聚体结构是独特的。
The stand-alone RAM (regulation of amino-acid metabolism) domain protein SraA from Thermus thermophilus HB8 (TTHA0845) was crystallized in the presence of zinc ions. The X-ray crystal structure was determined using a multiple-wavelength anomalous dispersion technique and was refined at 2.4 A resolution to a final R factor of 25.0%. The monomeric structure is a betaalphabetabetaalphabeta fold and it dimerizes mainly through interactions between the antiparallel beta-sheets. Furthermore, five SraA dimers form a ring with external and internal diameters of 70 and 20 A, respectively. This decameric structure is unique compared with the octameric and dodecameric structures found for other stand-alone RAM-domain proteins and the C-terminal RAM domains of Lrp/AsnC-family proteins.