SEQUENCE-IMPOSED STRUCTURAL CONSTRAINTS IN THE TONB PROTEIN OF ESCHERICHIA-COLI
SEQUENCE-IMPOSED STRUCTURAL CONSTRAINTS IN THE TONB PROTEIN OF ESCHERICHIA-COLI
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DOI：
10.1016/0014-5793(86)81020-1
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发表时间：
1986-11-24
期刊：
影响因子：
3.5
通讯作者：
HIGGINS, CF
中科院分区：
文献类型：
--
作者：
EVANS, JS;LEVINE, BA;HIGGINS, CF
使用高分辨率质子磁共振技术研究了源自 TonB 蛋白的 33 个残基肽片段的溶液构象，该蛋白参与细菌膜转运过程。这种富含脯氨酸的肽具有序列赋予的细长二级结构部分，必须保留天然蛋白质构型。这些结构限制提供了刚性元素，这意味着 TonB 具有纯粹的结构作用，并且与蛋白质的亚细胞位置和生物学作用相关。根据这些数据，我们认为该蛋白跨越了连接 TonB 依赖性转运系统的内膜和外膜成分的周质空间。
The solution conformation of a 33-residue peptide segment derived from the TonB protein which is implicated in bacterial membrane transport processes, has been investigated using high-resolution proton magnetic resonance techniques. This proline-rich peptide possesses sequence-imposed sections of elongated secondary structure that must be retained in the native protein configuration. These structural constraints provide elements of stiffness that imply a purely structural role for TonB and are relevant to the subcellular location and biological role of the protein. On the basis of these data we suggest that this protein spans the periplasmic space linking the inner and outer membrane components of TonB-dependent transport systems.