5ebc
From Proteopedia
Crystal structure of EccB1 of Mycobacterium tuberculosis in spacegroup P21 (state III)
Structural highlights
FunctionECCB1_MYCTU Part of the ESX-1 specialized secretion system, which delivers several virulence factors to host cells during infection, including the key virulence factors EsxA (ESAT-6) and EsxB (CFP-10).[1] Publication Abstract from PubMedThe 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. Crystallographic observation of the movement of the membrane-distal domain of the T7SS core component EccB1 from Mycobacterium tuberculosis.,Xie XQ, Zhang XL, Qi C, Li de F, Fleming J, Wang da C, Bi LJ Acta Crystallogr F Struct Biol Commun. 2016 Feb 1;72(Pt 2):139-44. doi:, 10.1107/S2053230X16000212. Epub 2016 Jan 22. PMID:26841765[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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