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. 2016 Dec 6;7(6):e01994-16. doi: 10.1128/mBio.01994-16

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Copyright © 2016 Hockenberry et al.

This is an open-access article distributed under the terms of the Creative Commons Attribution 4.0 International license.

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FIG 1 — PilT_L201C forms a hexamer but has reduced ability to bind and hydrolyze ATP. (A) Predicted structure of the N. gonorrhoeae PilT monomer (left), close-up view of its ATP binding site (top right), and residues of the Walker B domain of wt PilT and PilT_L201C (bottom right). Walker A domain (magenta); Walker B domain (blue); L201 side chain (orange). (B) Migration of purified PilT and PilT_L201C in a nondenaturing 6.5% acrylamide gel stained with Coomassie blue. Predicted molecular mass of the PilT hexamer is 222 kDa. (C) ATPase activity, V_max, and K_m values of PilT and PilT_L201C hexamers. Values are the average results from 3 independent experiments, each performed in triplicate. **, P < 0.01, Student’s two-tailed unpaired t test.