The S-layer homology domains of Paenibacillus alvei surface protein SpaA bind to cell wall polysaccharide through the terminal monosaccharide residue.
S-layer
SLH domain
X-ray crystallography
cell wall anchoring
isothermal titration calorimetry
secondary cell wall polymer
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
04 2022
04 2022
Historique:
received:
16
12
2021
revised:
16
02
2022
accepted:
17
02
2022
pubmed:
22
2
2022
medline:
27
4
2022
entrez:
21
2
2022
Statut:
ppublish
Résumé
Self-assembling (glyco)protein surface layers (S-layers) are ubiquitous prokaryotic cell-surface structures involved in structural maintenance, nutrient diffusion, host adhesion, virulence, and other processes, which makes them appealing targets for therapeutics and biotechnological applications as biosensors or drug delivery systems. However, unlocking this potential requires expanding our understanding of S-layer properties, especially the details of surface-attachment. S-layers of Gram-positive bacteria often are attached through the interaction of S-layer homology (SLH) domain trimers with peptidoglycan-linked secondary cell wall polymers (SCWPs). Cocrystal structures of the SLH domain trimer from the Paenibacillus alvei S-layer protein SpaA (SpaA
Identifiants
pubmed: 35189140
pii: S0021-9258(22)00185-5
doi: 10.1016/j.jbc.2022.101745
pmc: PMC8942822
pii:
doi:
Substances chimiques
Ligands
0
Membrane Glycoproteins
0
Membrane Proteins
0
Monosaccharides
0
Polysaccharides
0
S-layer proteins
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
101745Subventions
Organisme : Austrian Science Fund FWF
ID : W 1224
Pays : Austria
Informations de copyright
Copyright © 2022 The Authors. Published by Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Conflict of interest The authors declare that they have no conflicts of interest with the contents of this article.