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. 2010 Dec 21;67(Pt 1):23–26. doi: 10.1107/S174430911004443X

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© Nylander et al. 2011

This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.

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Comparison of the SspB and SpaP BAR regions. (a) The BAR motif in the S. gordonii AgI/II protein SspB is the recognition site for P. gingivalis and consists of a helix (KKVQDLLKK) followed by an extended region (NITVK). A calcium ion (grey sphere) stabilizes the motif through interactions (broken lines) with three main chains, two side chains and a water molecule. The analogous region in S. mutans SpaP is composed of an α-helix (QEIRDVLSKA) followed by an extended region (GIRPK) which share only 40% sequence identity with S. gordonii SspB. The two proteins are superimposed and shown in stereo. SspB is shown in grey and SpaP in blue and yellow. The residues are labelled, with the SspB residues in italics. (b, c) Electrostatic surface comparison of the BAR regions in SspB and SpaP. The SspB BAR region (b) and the equivalent region in SpaP (c) generate very different electrostatic surfaces and thus a different recognition pattern.