PDBsum entry 6cwl

Sugar binding protein

PDB id: 6cwl

Contents

Protein chains

164 a.a.

146 a.a.

Ligands

FHY ×2

Waters ×83

PDB id:

6cwl

Name:

Sugar binding protein

Title:

Crystal structure of spaa-slh in complex with beta-d-glcnac-(1->3)-4, 6-pyr-beta-d-mannacome

Structure:

Surface (s-) layer glycoprotein. Chain: a, b. Fragment: slh domains (unp residues 21-193). Synonym: spaa. Engineered: yes

Source:

Paenibacillus alvei. Bacillus alvei. Organism_taxid: 44250. Gene: spaa. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

2.15Å R-factor: 0.218 R-free: 0.255

Authors:

R.J.Blackler,S.V.Evans

Key ref:

R.J.Blackler et al. (2018). Structural basis of cell wall anchoring by SLH domains in Paenibacillus alvei. Nat Commun, 9, 3120. PubMed id: 30087354

Date:

30-Mar-18 Release date: 15-Aug-18

Protein chain

C1JZ07  (C1JZ07_PAEAL) -  Surface (S-) layer glycoprotein from Paenibacillus alvei

Seq: 983 a.a.

Struc: 164 a.a.

Protein chain

C1JZ07  (C1JZ07_PAEAL) -  Surface (S-) layer glycoprotein from Paenibacillus alvei

Seq: 983 a.a.

Struc: 146 a.a.

Nat Commun 9:3120 (2018)

PubMed id: 30087354

Structural basis of cell wall anchoring by SLH domains in Paenibacillus alvei.

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.

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.