7R49

Crystal structure of the L. plantarum acyl carrier protein synthase (AcpS)in complex with D-alanyl carrier protein (DltC1)

Summary for 7R49

• Entry DOI: 10.2210/pdb7r49/pdb
• Descriptor: Holo-[acyl-carrier-protein] synthase, D-alanyl carrier protein 1, 4'-PHOSPHOPANTETHEINE, ... (5 entities in total)
• Functional Keywords: acyl carrier protein synthase, d-alanyl carrier protein, complex, d-alanylation, teichoic acids, cytosolic protein
• Biological source: Lactiplantibacillus plantarum subsp. plantarum NC8; More
• Total number of polymer chains: 6
• Total formula weight: 70021.51

Authors

Nikolopoulos, N.,Ravaud, S.,Simorre, J.P.,Grangeasse, C. (deposition date: 2022-02-08, release date: 2022-08-03, Last modification date: 2024-01-31)

Primary citation

Nikolopoulos, N.,Matos, R.C.,Courtin, P.,Ayala, I.,Akherraz, H.,Simorre, J.P.,Chapot-Chartier, M.P.,Leulier, F.,Ravaud, S.,Grangeasse, C.
DltC acts as an interaction hub for AcpS, DltA and DltB in the teichoic acid D-alanylation pathway of Lactiplantibacillus plantarum.
Sci Rep, 12:13133-13133, 2022

PubMed Abstract: Teichoic acids (TA) are crucial for the homeostasis of the bacterial cell wall as well as their developmental behavior and interplay with the environment. TA can be decorated by different modifications, modulating thus their biochemical properties. One major modification consists in the esterification of TA by D-alanine, a process known as D-alanylation. TA D-alanylation is performed by the Dlt pathway, which starts in the cytoplasm and continues extracellularly after D-Ala transportation through the membrane. In this study, we combined structural biology and in vivo approaches to dissect the cytoplasmic steps of this pathway in Lactiplantibacillus plantarum, a bacterial species conferring health benefits to its animal host. After establishing that AcpS, DltB, DltC1 and DltA are required for the promotion of Drosophila juvenile growth under chronic undernutrition, we solved their crystal structure and/or used NMR and molecular modeling to study their interactions. Our work demonstrates that the suite of interactions between these proteins is ordered with a conserved surface of DltC1 docking sequentially AcpS, DltA and eventually DltB. Altogether, we conclude that DltC1 acts as an interaction hub for all the successive cytoplasmic steps of the TA D-alanylation pathway.

PubMed: 35907949
DOI: 10.1038/s41598-022-17434-2

Experimental method

X-RAY DIFFRACTION (1.88 Å)