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铁转运蛋白FeoB截短的胞质结构域的结晶及初步X射线衍射分析

Crystallization and preliminary X-ray diffraction analysis of the truncated cytosolic domain of the iron transporter FeoB.

作者信息

Jin Yaohua, Hattori Motoyuki, Nisimasu Hiroshi, Ishitani Ryuichiro, Nureki Osamu

机构信息

Department of Chemical Engineering, Tsinghua University, Beijing 100084, People's Republic of China.

出版信息

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Aug 1;65(Pt 8):784-7. doi: 10.1107/S1744309109024464. Epub 2009 Jul 25.

Abstract

FeoB-family proteins are widely distributed in bacteria and archaea and are involved in high-affinity Fe(2+) uptake through the plasma membrane. FeoB consists of an N-terminal cytosolic region followed by a C-terminal transmembrane region. The cytosolic region contains small GTPase and GDP dissociation inhibitor-like domains, which serve a regulatory function. The truncated cytosolic region of the iron transporter FeoB from Thermotoga maritima was overexpressed, purified and crystallized. Four native or SeMet crystal forms in a nucleotide-free state or in complex with either GDP or GMPPNP diffracted to resolutions of between 1.5 and 2.1 A.

摘要

FeoB家族蛋白广泛分布于细菌和古细菌中,参与通过质膜进行的高亲和力Fe(2+)摄取。FeoB由一个N端胞质区域和一个C端跨膜区域组成。胞质区域包含小GTPase和GDP解离抑制剂样结构域,具有调节功能。来自嗜热栖热菌的铁转运蛋白FeoB的截短胞质区域被过量表达、纯化并结晶。四种处于无核苷酸状态或与GDP或GMPPNP结合的天然或SeMet晶体形式的衍射分辨率在1.5至2.1埃之间。

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