Crystallographic observation of the movement of the membrane-distal domain of the T7SS core component EccB1 from Mycobacterium tuberculosis

详细信息    查看全文

• 作者：Xiao-Qian Xie ; Xiao-Li Zhang ; Chao Qi ; De-Feng Li ; Joy Fleming ; Da-Cheng Wang and Li-Jun Bi
• 关键词：Rv3869 ; type VII secretion system ; Mycobacterium tuberculosis ; ESX-1
• 刊名：Acta Crystallographica Section F
• 出版年：2016
• 出版时间：February 2016
• 年：2016
• 卷：72
• 期：2
• 页码：139-144
• 全文大小：1019K
• ISSN：1744-3091

文摘

The protein EccB1, a core component of the type VII secretion system (T7SS) of Mycobacterium tuberculosis, has been identified as an ATPase and is essential for the secretion of virulence factors by the ESX-1 system. In a previous study, EccB1 structures were determined in two different conformations. Here, two new conformations are identified and described. These four conformations present snapshots of the swinging movement of the membrane-distal domain A2. The movement of this domain involves conformational changes in two flexible loops (loop A, residues 243–264, and loop B, residues 324–341) which are rich in proline and glycine residues and connect domain A2 to domains C1 and B2. It is proposed that the movement of this domain is related to the ATPase activity of EccB1 and its homologues, as well as to the substrate transport of ESX secretion systems.