Structural basis of cell wall anchoring by SLH domains in Paenibacillus alvei

Ryan J. Blackler, Arturo López-Guzmán, Fiona F. Hager, Bettina Janesch, Gudrun Martinz, Susannah M. L. Gagnon, Omid Haji-Ghassemi, Paul Kosma, Paul Messner, Christina Schäffer () and Stephen V. Evans ()
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Ryan J. Blackler: University of Victoria
Arturo López-Guzmán: Universität für Bodenkultur Wien
Fiona F. Hager: Universität für Bodenkultur Wien
Bettina Janesch: Universität für Bodenkultur Wien
Gudrun Martinz: Universität für Bodenkultur Wien
Susannah M. L. Gagnon: University of Victoria
Omid Haji-Ghassemi: University of Victoria
Paul Kosma: Universität für Bodenkultur Wien
Paul Messner: Universität für Bodenkultur Wien
Christina Schäffer: Universität für Bodenkultur Wien
Stephen V. Evans: University of Victoria

Nature Communications, 2018, vol. 9, issue 1, 1-11

Abstract: Abstract Self-assembling protein surface (S-) layers are common cell envelope structures of prokaryotes and have critical roles from structural maintenance to virulence. S-layers of Gram-positive bacteria are often attached through the interaction of S-layer homology (SLH) domain trimers with peptidoglycan-linked secondary cell wall polymers (SCWPs). Here we present an in-depth characterization of this interaction, with co-crystal structures of the three consecutive SLH domains from the Paenibacillus alvei S-layer protein SpaA with defined SCWP ligands. The most highly conserved SLH domain residue SLH-Gly29 is shown to enable a peptide backbone flip essential for SCWP binding in both biophysical and cellular experiments. Furthermore, we find that a significant domain movement mediates binding by two different sites in the SLH domain trimer, which may allow anchoring readjustment to relieve S-layer strain caused by cell growth and division.

Date: 2018
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-05471-3

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DOI: 10.1038/s41467-018-05471-3

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