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Crystallographic observation of the movement of the membrane‐distal domain of the T7SS core component EccB1 from Mycobacterium tuberculosis
Author(s) -
Xie Xiao-Qian,
Zhang Xiao-Li,
Qi Chao,
Li De-Feng,
Fleming Joy,
Wang Da-Cheng,
Bi Li-Jun
Publication year - 2016
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x16000212
Subject(s) - secretion , domain (mathematical analysis) , mycobacterium tuberculosis , loop (graph theory) , chemistry , virulence , glycine , membrane , component (thermodynamics) , crystallography , stereochemistry , biophysics , biology , biochemistry , tuberculosis , amino acid , physics , gene , mathematics , thermodynamics , medicine , mathematical analysis , pathology , combinatorics
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.