Functional complementation of SecA fragments with C-terminal fragment C34. Ying-hsin Hsieh Ying-ju Huang Hao Zhang Qian Liu Yang Lu Hsiuchin Yang John Houghton Chun Jiang Sen-Fang Sui Phang C. Tai 10.1371/journal.pone.0178307.g006 https://plos.figshare.com/articles/figure/Functional_complementation_of_SecA_fragments_with_C-terminal_fragment_C34_/5068711 <p>(A) Channel activity in SecA domains reconstituted with C34, SecA<sub>610-901</sub>. (B) Translocation activity in SecA domains reconstituted with C34. N609 together with C34 have no activity, and could serve as internal negative controls. The reactions were conducted with liposomes with SecYEG or SecYEG-SecDFC as indicated. 100% translocation activity is SecA with SecYEG-DFC.</p> 2017-06-02 17:37:16 N 831. SecA domain fragments SecA-only protein-conducting channels ion channel activity protein translocation capability N-terminal fragment SecAN 493 N-terminal domain fragments ATPase activity form multi-functional domains Sec-dependent translocation pathways N 619-N Lipids SecA domain fragment interactions pore structure form high-efficiency channels C-terminal deletion fragments protein translocation non-functional N-terminal fragments 643-N 901 aminoacyl residues SecYEG-SecDF protein translocation ability form SecA-only pore structures amino-acyl residues SecA 619-831 fragments N 608-N SecA form pore-ring structures C-terminal fragments complement