Callebaut I, Mornon J P
Laboratoire de Minéralogie-Cristallographie, CNRS URA09, Universités Paris 6, France.
FEBS Lett. 1995 Oct 30;374(2):211-5. doi: 10.1016/0014-5793(95)01109-r.
The trigger factor of Escherichia coli is known as a chaperone protein which forms soluble complexes with the precursor to outer membrane protein A and assists in the maintenance of translocation competence. Sequence analysis shows that trigger factor contains a domain belonging to the FK506-binding protein (FKBP) family and possessing all the amino acids necessary for FK506 binding and peptidyl-prolyl cis-trans isomerase (Ppiase) activity. Consequently, this protein could be directly involved in the unfolding/folding processes occurring during translocation across the E. coli plasma membrane and, more generally, in facilitating protein folding. The central position of the FKBP domain within the trigger factor sequence as well as several original features of the loops surrounding the FK506-binding pocket are not found in any other FKBPs, making it undetectable by the Fkbp-Ppiase signature patterns.
大肠杆菌的触发因子是一种伴侣蛋白，它与外膜蛋白A的前体形成可溶性复合物，并协助维持转运能力。序列分析表明，触发因子包含一个属于FK506结合蛋白（FKBP）家族的结构域，具有FK506结合和肽基脯氨酰顺反异构酶（Ppiase）活性所需的所有氨基酸。因此，这种蛋白质可能直接参与大肠杆菌质膜转运过程中发生的解折叠/折叠过程，更普遍地说，参与促进蛋白质折叠。FKBP结构域在触发因子序列中的中心位置以及围绕FK506结合口袋的环的几个原始特征在任何其他FKBP中都未发现，这使得它无法通过Fkbp-Ppiase特征模式检测到。
