%0 Journal Article
%T A Minimum of Three Motifs Is Essential for Optimal Binding of Pseudomurein Cell Wall-Binding Domain of Methanothermobacter thermautotrophicus
%A Ganesh Ram R. Visweswaran
%A Bauke W. Dijkstra
%A Jan Kok
%J PLOS ONE
%D 2012
%I Public Library of Science (PLoS)
%R 10.1371/journal.pone.0021582
%X We have biochemically and functionally characterized the pseudomurein cell wall-binding (PMB) domain that is present at the C-terminus of the Surface (S)-layer protein MTH719 from Methanothermobacter thermautotrophicus. Chemical denaturation of the protein with guanidinium hydrochloride occurred at 3.8 M. A PMB-GFP fusion protein not only binds to intact pseudomurein of methanogenic archaea, but also to spheroplasts of lysozyme-treated bacterial cells. This binding is pH dependent. At least two of the three motifs that are present in the domain are necessary for binding. Limited proteolysis revealed a possible cleavage site in the spacing sequence between motifs 1 and 2 of the PMB domain, indicating that the motif region itself is protected from proteases.
%U http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0021582