Molecular mechanism of transmembrane signaling by the aspartate receptor: A model
Molecular mechanism of transmembrane signaling by the aspartate receptor: A model
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DOI：
10.1073/pnas.93.6.2545
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发表时间：
1996-03-19
影响因子：
11.1
通讯作者：
Falke, JJ
中科院分区：
文献类型：
--
作者：
Chervitz, SA;Falke, JJ
细菌趋化性的天冬氨酸受体是在原核和真核生物中发现的一大类跨膜受体的代表。这些受体，调节组氨酸激酶途径，并具有两个假定的跨膜螺旋每个亚基，似乎控制各种各样的细胞过程。双螺旋受体类的最佳特征亚组是来自大肠杆菌和鼠伤寒沙门氏菌的化学感受受体的同源家族，包括天冬氨酸受体。这种受体结合天冬氨酸，引诱剂，在周质区室，并经历了分子内，跨膜构象变化，从而调节结合组氨酸激酶在细胞质中的自磷酸化速率。在这里，我们分析了最近的结果，从X-射线晶体学，解决F-19 NMR，和工程二硫化物的研究探测内的受体的周质和跨膜区域的酒石酸诱导的结构变化。总之，这些方法提供了证据表明，天冬氨酸结合触发了第二跨膜螺旋的“摆动活塞”位移，这被认为是跨双层传递信号。
The aspartate receptor of bacterial chemotaxis is representative of a large class of membrane-spanning receptors found in prokaryotic and eukaryotic organisms. These receptors, which regulate histidine kinase pathways and possess two putative transmembrane helices per subunit, appear to control a wide variety of cellular processes. The best characterized subgroup of the two helix receptor class is the homologous family of chemosensory receptors from Escherichia coli and Salmonella typhimurium, including the aspartate receptor. This receptor binds aspartate, an attractant, in the periplasmic compartment and undergoes an intramolecular, transmembrane conformational change, thereby modulating the autophosphorylation rate of a bound histidine kinase in the cytoplasm. Here, we analyze recent results from x-ray crystallographic, solution F-19 NMR, and engineered disulfide studies probing the aspartate-induced structural change within the periplasmic and transmembrane regions of the receptor. Together, these approaches provide evidence that aspartate binding triggers a ''swinging-piston'' displacement of the second membrane-spanning helix, which is proposed to communicate the signal across the bilayer.