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PDBsum entry 6cwl
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Sugar binding protein
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PDB id
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6cwl
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References listed in PDB file
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Key reference
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Title
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Structural basis of cell wall anchoring by slh domains in paenibacillus alvei.
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Authors
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R.J.Blackler,
A.López-Guzmán,
F.F.Hager,
B.Janesch,
G.Martinz,
S.M.L.Gagnon,
O.Haji-Ghassemi,
P.Kosma,
P.Messner,
C.Schäffer,
S.V.Evans.
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Ref.
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Nat Commun, 2018,
9,
3120.
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PubMed id
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Abstract
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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.
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