晶体结构的趋化作用受体甲基转移酶雪儿表明绑定S-adenosylmethionine守恒的结构图案。
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Djordjevic年代,股票
晶体结构的趋化作用受体甲基转移酶雪儿表明绑定S-adenosylmethionine守恒的结构图案。
结构。1997年4月15日,5 (4):545 - 58。
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9115443 (在PubMed]
- 文摘
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背景:鞭毛细菌游到有利的化学物质,远离有害的。chemoeffector梯度的感应包括趋化性受体,跨膜蛋白,通过周质的检测刺激域和通过胞质域下游信号转导信号组件。信号输出的趋化作用受体影响通过绑定chemoeffector配体的周质的领域和特定的谷氨酸残基的甲基化的胞质域受体。雪儿的甲基化是催化S-adenosylmethionine-dependent甲基转移酶。雪儿形成紧密的复杂与受体通过绑定一个地区受体不同的甲基化的网站。雪儿属于一类广泛的甲基化酶参与多种基质。直到现在,没有类的结构蛋白甲基转移酶的特点。结果:鼠伤寒沙门氏菌趋化作用受体结构的甲基转移酶雪儿绑定到S-adenosylhomocysteine,产品和抑制剂的甲基化反应,已经确定在2.0一项决议。两个域蛋白质结构揭示了雪儿,与一个较小的氨基端螺旋域连接通过一个多肽连接到更大的c端α/β域。c端域nucleotide-binding褶皱的特征,用一个插入一个小反平行的β表子域名。 The S-adenosylhomocysteine-binding site is formed mainly by the large domain, with contributions from residues within the N-terminal domain and the linker region. CONCLUSIONS: The CheR structure shares some structural similarities with small molecule DNA and RNA methyltransferases, despite a lack of sequence similarity among them. In particular, there is significant structural preservation of the S-adenosylmethionine-binding clefts; the specific length and conformation of a loop in the alpha/beta domain seems to be required for S-adenosylmethionine binding within these enzymes. Unique structural features of CheR, such as the beta subdomain, are probably necessary for CheR's specific interaction with its substrates, the bacterial chemotaxis receptors.