6CWR

Crystal structure of SpaA-SLH/G46A/G109A in complex with 4,6-Pyr-beta-D-ManNAcOMe

Summary for 6CWR

• Entry DOI: 10.2210/pdb6cwr/pdb
• Related: 6CWC 6CWF 6CWH 6CWI 6CWL 6CWM 6CWN
• Descriptor: Surface (S-) layer glycoprotein, methyl 2-(acetylamino)-4,6-O-[(1S)-1-carboxyethylidene]-2-deoxy-beta-D-mannopyranoside (3 entities in total)
• Functional Keywords: surface layer homology domain, secondary cell wall polymer, s-layer, slh, scwp, sugar binding protein
• Biological source: Paenibacillus alvei (Bacillus alvei)
• Total number of polymer chains: 1
• Total formula weight: 20117.57

Authors

Blackler, R.J.,Gagnon, S.M.L.,Haji-Ghassemi, O.,Evans, S.V. (deposition date: 2018-03-30, release date: 2018-08-15, Last modification date: 2023-10-04)

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 (1.24 Å)