6CWC

Crystal structure of SpaA-SLH

Summary for 6CWC

• Entry DOI: 10.2210/pdb6cwc/pdb
• Related: 6CWF 6CWH 6CWI 6CWL 6CWM 6CWN 6CWR
• Descriptor: Surface (S-) layer glycoprotein, SULFATE ION, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: surface layer homology domain, s-layer, slh, sugar binding protein
• Biological source: Paenibacillus alvei (Bacillus alvei)
• Total number of polymer chains: 2
• Total formula weight: 39831.51

Authors

Blackler, R.J.,Evans, S.V. (deposition date: 2018-03-30, release date: 2018-08-15, Last modification date: 2024-03-13)

Primary citation

Blackler, R.J.,Lopez-Guzman, A.,Hager, F.F.,Janesch, B.,Martinz, G.,Gagnon, S.M.L.,Haji-Ghassemi, O.,Kosma, P.,Messner, P.,Schaffer, C.,Evans, S.V.
Structural basis of cell wall anchoring by SLH domains in Paenibacillus alvei.
Nat Commun, 9:3120-3120, 2018

PubMed 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.

PubMed: 30087354
DOI: 10.1038/s41467-018-05471-3

Experimental method

X-RAY DIFFRACTION (1.9 Å)