8AIK
Crystal structure of DltE from L. plantarum, tartare bound form
8AIK の概要
エントリーDOI | 10.2210/pdb8aik/pdb |
分子名称 | Beta-lactamase family protein, L(+)-TARTARIC ACID (3 entities in total) |
機能のキーワード | carboxyesterase, d-alanylation, lipoteichoic acids, cell cycle |
由来する生物種 | Lactiplantibacillus plantarum |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 84095.28 |
構造登録者 | |
主引用文献 | 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 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: 37042660DOI: 10.7554/eLife.84669 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.95 Å) |
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