8AIK

Crystal structure of DltE from L. plantarum, tartare bound form

Summary for 8AIK

• Entry DOI: 10.2210/pdb8aik/pdb
• Descriptor: Beta-lactamase family protein, L(+)-TARTARIC ACID (3 entities in total)
• Functional Keywords: carboxyesterase, d-alanylation, lipoteichoic acids, cell cycle
• Biological source: Lactiplantibacillus plantarum
• Total number of polymer chains: 2
• Total formula weight: 84095.28

Authors

Ravaud, S.,Nikolopoulos, N.,Grangeasse, C. (deposition date: 2022-07-26, release date: 2023-04-26, Last modification date: 2024-02-07)

Primary citation

Nikolopoulos, N.,Matos, R.,Ravaud, S.,Courtin, P.,Akherraz, H.,Palussiere, S.,Gueguen-Chaignon, V.,Salomon-Mallet, M.,Guillot, A.,Guerardel, Y.,Chapot-Chartier, M.P.,Grangeasse, C.,Leulier, F.
Structure-function analysis of Lactiplantibacillus plantarum DltE& reveals D-alanylated lipoteichoic acids as direct cues supporting Drosophila juvenile growth.
Elife, 12:-, 2023

PubMed Abstract: Metazoans establish mutually beneficial interactions with their resident microorganisms. However, our understanding of the microbial cues contributing to host physiology remains elusive. Previously, we identified a bacterial machinery encoded by the operon involved in 's juvenile growth promotion by . Here, using crystallography combined with biochemical and cellular approaches, we investigate the physiological role of an uncharacterized protein (DltE) encoded by this operon. We show that lipoteichoic acids (LTAs) but not wall teichoic acids are D-alanylated in cell envelope and demonstrate that DltE is a D-Ala carboxyesterase removing D-Ala from LTA. Using the mutualistic association of and as a symbiosis model, we establish that D-alanylated LTAs (D-Ala-LTAs) are direct cues supporting intestinal peptidase expression and juvenile growth in . Our results pave the way to probing the contribution of D-Ala-LTAs to host physiology in other symbiotic models.

PubMed: 37042660
DOI: 10.7554/eLife.84669

Experimental method

X-RAY DIFFRACTION (1.95 Å)