5NXK

L. reuteri 53608 SRRP

Summary for 5NXK

• Entry DOI: 10.2210/pdb5nxk/pdb
• Descriptor: Serine-rich secreted cell wall anchored (LPXTG-motif ) protein (2 entities in total)
• Functional Keywords: beta-solenoid, l. reuteri, adhesin, cell adhesion
• Biological source: Lactobacillus reuteri ATCC 53608
• Total number of polymer chains: 3
• Total formula weight: 98965.71

Authors

Sequeira, S.,Dong, C. (deposition date: 2017-05-10, release date: 2018-03-21, Last modification date: 2024-05-08)

Primary citation

Sequeira, S.,Kavanaugh, D.,MacKenzie, D.A.,Suligoj, T.,Walpole, S.,Leclaire, C.,Gunning, A.P.,Latousakis, D.,Willats, W.G.T.,Angulo, J.,Dong, C.,Juge, N.
Structural basis for the role of serine-rich repeat proteins from Lactobacillus reuteriin gut microbe-host interactions.
Proc. Natl. Acad. Sci. U.S.A., 115:E2706-E2715, 2018

PubMed Abstract: , a Gram-positive bacterial species inhabiting the gastrointestinal tract of vertebrates, displays remarkable host adaptation. Previous mutational analyses of rodent strain 100-23C identified a gene encoding a predicted surface-exposed serine-rich repeat protein (SRRP) that was vital for biofilm formation in mice. SRRPs have emerged as an important group of surface proteins on many pathogens, but no structural information is available in commensal bacteria. Here we report the 2.00-Å and 1.92-Å crystal structures of the binding regions (BRs) of SRRP and SRRP from ATCC 53608, revealing a unique β-solenoid fold in this important adhesin family. SRRP-BR bound to host epithelial cells and DNA at neutral pH and recognized polygalacturonic acid (PGA), rhamnogalacturonan I, or chondroitin sulfate A at acidic pH. Mutagenesis confirmed the role of the BR putative binding site in the interaction of SRRP-BR with PGA. Long molecular dynamics simulations showed that SRRP-BR undergoes a pH-dependent conformational change. Together, these findings provide mechanistic insights into the role of SRRPs in host-microbe interactions and open avenues of research into the use of biofilm-forming probiotics against clinically important pathogens.

PubMed: 29507249
DOI: 10.1073/pnas.1715016115

Experimental method

X-RAY DIFFRACTION (1.918 Å)