9XZN
Teichoic acid flippase TacF from Streptococcus pneumoniae
Summary for 9XZN
| Entry DOI | 10.2210/pdb9xzn/pdb |
| EMDB information | 72367 |
| Descriptor | Soluble cytochrome b562,Teichoic acid subunit flippase (1 entity in total) |
| Functional Keywords | teichoic acid, flippase, transporter, lipid transport, membrane protein |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 1 |
| Total formula weight | 67575.09 |
| Authors | Cebrero, G.,Chidananda, H.A.,Denereaz, J.L.,Cester, E.,Mathew, A.T.,Bhowmik, D.R.,Capitani, M.,Reymond, J.L.,Kannan, N.,Veening, J.W.,Mehdipour, A.R.,Perez, C. (deposition date: 2025-08-27, release date: 2026-04-29, Last modification date: 2026-05-20) |
| Primary citation | Cebrero, G.,Chidananda, A.H.,Cester, E.,Denereaz, J.,Demir, E.S.,Mathew, A.T.,Bhowmik, D.R.,de Capitani, M.,Reymond, J.L.,Kannan, N.,Avci, F.Y.,Veening, J.W.,Mehdipour, A.R.,Perez, C. Mechanistic basis of teichoic acid transport by a gatekeeper flippase. Biorxiv, 2026 Cited by PubMed Abstract: The cell wall is a complex structure that protects bacteria from environmental threats. Phosphocholine-containing teichoic acids are key cell wall biopolymers critical for host colonization, immune evasion, competence, and persistence in . The flippase TacF, a member of the multidrug/oligosaccharide-lipid/polysaccharide (MOP) superfamily, monitors the phosphocholine content of teichoic acids during transport, yet the underlying mechanism of this process remains unknown. We present a cryo-EM structure of TacF in lipid nanodiscs. complementation assays and molecular dynamics simulations reveal key residues involved in teichoic acid recognition and transport, while coevolutionary and conservation analyses delineate common mechanistic elements among MOP flippases, indicating a shared mechanism for polyprenyl-diphosphate-linked oligosaccharide lipid transport. Our findings provide mechanistic insights into an essential flippase involved in pathogenesis and a potential drug target. PubMed: 41808984DOI: 10.64898/2026.02.22.707263 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.63 Å) |
Structure validation
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