Open AccessCloning, purification and crystallization of MotB, a stator component of the proton‐driven bacterial flagellar motor
Author(s) -
O'Neill Jenna,
Roujeinikova Anna
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108012219
Subject(s) - periplasmic space , stator , crystallography , flagellum , ammonium sulfate , protein subunit , proton , materials science , transmembrane protein , peptidoglycan , chemistry , biophysics , escherichia coli , physics , biochemistry , cell wall , biology , chromatography , receptor , quantum mechanics , gene
MotB is an essential component of the proton motive force‐driven bacterial flagellar motor. It binds to the stress‐bearing layer of peptidoglycan in the periplasm, anchoring the MotA/MotB stator unit to the cell wall. Proton flow through the channel formed by the transmembrane helices of MotA and MotB generates the turning force (torque) applied to the rotor. Crystals of recombinant Helicobacter pylori MotB have been obtained by the sitting‐drop vapour‐diffusion method using ammonium sulfate as a precipitant. These crystals belong to space group P 4 1 2 1 2 or its enantiomorph P 4 3 2 1 2, with unit‐cell parameters a = 75.2, b = 75.2, c = 124.7 Å. The asymmetric unit appears to contain one subunit, corresponding to a packing density of 3.4 Å 3 Da −1 . The crystals diffract X‐rays to at least 1.8 Å resolution on a synchrotron‐radiation source.