9XGLSummary for 9XGL
| Entry DOI | 10.2210/pdb9xgl/pdb |
| Descriptor | D-alanyl carrier protein (2 entities in total) |
| Functional Keywords | ligase, structural protein |
| Biological source | Staphylococcus aureus subsp. aureus Mu50 |
| Total number of polymer chains | 4 |
| Total formula weight | 36276.58 |
| Authors | Jeon, H.,Lee, I.-G. (deposition date: 2025-10-30, release date: 2026-01-21, Last modification date: 2026-02-11) |
| Primary citation | Jeon, H.,Lee, H.,Song, C.,Lee, I.G. Structural Insights into the Staphylococcus aureus DltC-Mediated D-Alanine Transfer. Biomolecules, 16:-, 2025 Cited by PubMed Abstract: () is a major Gram-positive pathogen, and treatment of infections is often challenging due to widespread antibiotic resistance. In Gram-positive bacteria such as , D-alanylation of teichoic acids (TA) reduces the net negative charge of the cell envelope and contributes to resistance to diverse antibiotics, particularly cationic antimicrobial peptides. D-alanylation is mediated by the ABCD operon, which encodes four proteins (DltA, DltB, DltC, and DltD), all of which is essential for the multistep transfer of D-alanine to teichoic acids. Here, we present the first crystal structure of the D-alanyl carrier protein DltC and analyze its interaction with DltA using AlphaFold3 and all-atom molecular dynamics simulations. We further show that single substitutions of DltA-DltC interface residues abolish DltC mediated enhancement of DltA catalysis. Together, these findings define a catalytically critical DltA-DltC interface and provide a structural insight for targeting the D-alanylation pathway as a potential anti- strategy. PubMed: 41594584DOI: 10.3390/biom16010044 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.28 Å) |
Structure validation
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