6CWI
Crystal structure of SpaA-SLH in complex with 4,6-Pyr-beta-D-ManNAcOMe (C2)
Summary for 6CWI
| Entry DOI | 10.2210/pdb6cwi/pdb |
| Related | 6CWC 6CWF 6CWH 6CWL 6CWM 6CWN 6CWR |
| Descriptor | Surface (S-) layer glycoprotein, methyl 2-(acetylamino)-4,6-O-[(1S)-1-carboxyethylidene]-2-deoxy-beta-D-mannopyranoside, SULFATE ION, ... (4 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 | 2 |
| Total formula weight | 40676.45 |
| Authors | Blackler, R.J.,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 Cited by 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: 30087354DOI: 10.1038/s41467-018-05471-3 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.16 Å) |
Structure validation
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