8jes | pdb_00008jes

Cryo-EM structure of DltB homo-tetramer

spinqualitylabelsall models 8jes, resolution 3.42Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8jes is a 4 chain structure with sequence from Streptococcus thermophilus LMG 18311. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.42Å Ligands: DGA, LMT, PGT Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function DLTB_STRT2 O-acyltransferase that catalyzes D-alanylation of both teichoic acid and lipoteichoic acid (LTA) (PubMed:30283133). D-alanylation of LTA plays an important role in modulating the properties of the cell wall in Gram-positive bacteria, influencing the net charge of the cell wall (PubMed:30283133). Catalyzes D-alanylation from DltC carrier protein (PubMed:30283133). Publication Abstract from PubMed DltB, a model member of the Membrane-Bound O-AcylTransferase (MBOAT) superfamily, plays a crucial role in D-alanylation of the lipoteichoic acid (LTA), a significant component of the cell wall of gram-positive bacteria. This process stabilizes the cell wall structure, influences bacterial virulence, and modulates the host immune response. Despite its significance, the role of DltB is not well understood. Through biochemical analysis and cryo-EM imaging, we discover that Streptococcus thermophilus DltB forms a homo-tetramer on the cell membrane. We further visualize DltB in an apo form, in complex with DltC, and in complex with its inhibitor amsacrine (m-AMSA). Each tetramer features a central hole. The C-tunnel of each protomer faces the intratetramer interface and provides access to the periphery membrane. Each protomer binds a DltC without changing the tetrameric organization. A phosphatidylglycerol (PG) molecule in the substrate-binding site may serve as an LTA carrier. The inhibitor m-AMSA bound to the L-tunnel of each protomer blocks the active site. The tetrameric organization of DltB provides a scaffold for catalyzing D-alanyl transfer and regulating the channel opening and closing. Our findings unveil DltB's dual function in the D-alanylation pathway, and provide insight for targeting DltB as a anti-virulence antibiotic. Structural insights into the transporting and catalyzing mechanism of DltB in LTA D-alanylation.,Zhang P, Liu Z Nat Commun. 2024 Apr 22;15(1):3404. doi: 10.1038/s41467-024-47783-7. PMID:38649359 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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