5EBC

Crystal structure of EccB1 of Mycobacterium tuberculosis in spacegroup P21 (state III)

Summary for 5EBC

• Entry DOI: 10.2210/pdb5ebc/pdb
• Related: 3X3M 3X3N 5EBD
• Descriptor: ESX-1 secretion system protein eccB1, CALCIUM ION (2 entities in total)
• Functional Keywords: alpha-beta-alpha sandwich, beta-sheet, atpase, protein transport, t7ss, esx-1 secretion system
• Biological source: Mycobacterium tuberculosis
• Cellular location: Cell inner membrane ; Single- pass membrane protein : P9WNR7
• Total number of polymer chains: 1
• Total formula weight: 45744.82

Authors

Zhang, X.L.,Qi, C.,Xie, X.Q.,Li, D.F.,Bi, L.J. (deposition date: 2015-10-19, release date: 2016-02-17, Last modification date: 2023-11-08)

Primary citation

Xie, X.Q.,Zhang, X.L.,Qi, C.,Li, D.F.,Fleming, J.,Wang, D.C.,Bi, L.J.
Crystallographic observation of the movement of the membrane-distal domain of the T7SS core component EccB1 from Mycobacterium tuberculosis.
Acta Crystallogr.,Sect.F, 72:139-144, 2016

PubMed Abstract: 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.

PubMed: 26841765
DOI: 10.1107/S2053230X16000212

Experimental method

X-RAY DIFFRACTION (3 Å)