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EssC: domain structures inform on the elusive translocation channel in the Type VII secretion system.

Biochem J. 2016; 
Zoltner M, Ng WM, Money JJ, Fyfe PK, Kneuper H, Palmer T, Hunter WN.
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Custom Vector Construction coli K12 (Genscript)] was cloned into the NcoI/XhoI site of a modified pET27b vector (Novagen) creating pET27bEssC. Get A Quote

摘要

The membrane-bound protein EssC is an integral component of the bacterial Type VII secretion system (T7SS), which is a determinant of virulence in important Gram-positive pathogens. The protein is predicted to consist of an intracellular repeat of forkhead-associated (FHA) domains at the N-terminus, two transmembrane helices and three P-loop-containing ATPase-type domains, D1-D3, forming the C-terminal intracellular segment. We present crystal structures of the N-terminal FHA domains (EssC-N) and a C-terminal fragment EssC-C from Geobacillus thermodenitrificans, encompassing two of the ATPase-type modules, D2 and D3. Module D2 binds ATP with high affinity whereas D3 does not. The EssC-N and EssC-C constructs a... More

关键词

ATPase; ESX-1; P-loop-containing domain; forkhead-associated domain; membrane-bound protein; secretion system