2015
DOI: 10.1096/fj.15-270843
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Abstract: Pathogenic mycobacteria transport virulence factors across their complex cell wall via a type VII secretion system (T7SS)/early secreted antigenic target-6 of kDa secretion system (ESX). ESX conserved component (Ecc) B, a core component of the T7SS architecture, is predicted to be a membrane bound protein, but little is known about its structure and function. Here, we characterize EccB1, showing that it is an ATPase with no sequence or structural homology to other ATPases located in the cell envelope of Mycoba… Show more

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Cited by 26 publications
(28 citation statements)
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“…To know the structural differences of the EccB 5 protein, prediction of the 3D protein models was done based on the database obtained from Swiss model and compared the structure of mutant and wild type using 3x3n template. 19 The mutated region showed b-strand structure, while the wild type showed the loop structure prediction. These changes may be due to the changes in amino acid residues Asn426, which has hydrophilic side chain to Ile426, which has hydrophobic side groups.…”
Section: Discussionmentioning
confidence: 99%
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“…To know the structural differences of the EccB 5 protein, prediction of the 3D protein models was done based on the database obtained from Swiss model and compared the structure of mutant and wild type using 3x3n template. 19 The mutated region showed b-strand structure, while the wild type showed the loop structure prediction. These changes may be due to the changes in amino acid residues Asn426, which has hydrophilic side chain to Ile426, which has hydrophobic side groups.…”
Section: Discussionmentioning
confidence: 99%
“…17,18 The protein model of EccB 5 was built using 3x3n for template. 19 Transmembrane helices proteins region prediction was used to check and confirm the protein structural details. 20,21…”
Section: Protein Prediction and Determination Of Transmembrane Proteinmentioning
confidence: 99%
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“…Structural and functional information has been reported for truncated and isolated, soluble domains of the ESX translocon complexes and their homologs ( 1215 ). A low resolution, negative stain electron microscopy structure of ESX-5 shows the translocon complex assembles into a hexamer ( 16 ).…”
Section: Main Textmentioning
confidence: 99%