6cwl

Crystal structure of SpaA-SLH in complex with beta-D-GlcNAc-(1->3)-4,6-Pyr-beta-D-ManNAcOMe

spinqualitylabelsall models 6cwl, resolution 2.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6cwl is a 2 chain structure with sequence from Paenibacillus alvei. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.15Å Ligands: FHY Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function C1JZ07_PAEAL Publication Abstract from PubMed 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. Structural basis of cell wall anchoring by SLH domains in Paenibacillus alvei.,Blackler RJ, Lopez-Guzman A, Hager FF, Janesch B, Martinz G, Gagnon SML, Haji-Ghassemi O, Kosma P, Messner P, Schaffer C, Evans SV Nat Commun. 2018 Aug 7;9(1):3120. doi: 10.1038/s41467-018-05471-3. PMID:30087354 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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