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8AJI

Crystal structure of DltE from L. plantarum, TCEP form

Summary for 8AJI
Entry DOI10.2210/pdb8aji/pdb
DescriptorBeta-lactamase family protein, 3,3',3''-phosphanetriyltripropanoic acid, L(+)-TARTARIC ACID, ... (5 entities in total)
Functional Keywordscarboxyesterase, d-alanylation, lipoteichoic acids, cell cycle
Biological sourceLactiplantibacillus plantarum
Total number of polymer chains4
Total formula weight169225.40
Authors
Ravaud, S.,Nikolopoulos, N.,Grangeasse, C. (deposition date: 2022-07-28, release date: 2023-04-26, Last modification date: 2024-02-07)
Primary citationNikolopoulos, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.94 Å)
Structure validation

238895

数据于2025-07-16公开中

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