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| Title | High-affinity PQQ import is widespread in Gram-negative bacteria. |
|---|---|
| Journal, issue, pages | Sci Adv, Vol. 11, Issue 22, Page eadr2753, Year 2025 |
| Publish date | May 30, 2025 |
Authors | Fabian Munder / Marcos Voutsinos / Klaus Hantke / Hari Venugopal / Rhys Grinter / ![]() |
| PubMed Abstract | Pyrroloquinoline quinone (PQQ) is a soluble redox cofactor used by diverse bacteria. Many Gram-negative bacteria that encode PQQ-dependent enzymes do not produce it and instead obtain it from the ...Pyrroloquinoline quinone (PQQ) is a soluble redox cofactor used by diverse bacteria. Many Gram-negative bacteria that encode PQQ-dependent enzymes do not produce it and instead obtain it from the environment. To achieve this, uses the TonB-dependent transporter PqqU as a high-affinity PQQ importer. Here, we show that PqqU binds PQQ with high affinity and determine the high-resolution structure of the PqqU-PQQ complex, revealing that PqqU undergoes conformational changes in PQQ binding to capture the cofactor in an internal cavity. We show that these conformational changes preclude the binding of a bacteriophage, which targets PqqU as a cell surface receptor. Guided by the PqqU-PQQ structure, we identify amino acids essential for PQQ import and leverage this information to map the presence of PqqU across Gram-negative bacteria. This reveals that PqqU is encoded by Gram-negative bacteria from at least 22 phyla occupying diverse habitats, indicating that PQQ is an important cofactor for bacteria that adopt diverse lifestyles and metabolic strategies. |
External links | Sci Adv / PubMed:40446051 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 1.99 Å |
| Structure data | EMDB-45192, PDB-9c4o: |
| Chemicals | ![]() ChemComp-CA: ![]() ChemComp-PQQ: ![]() ChemComp-HOH: |
| Source |
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Keywords | MEMBRANE PROTEIN / TonD-dependent / outer membrane / transporter / PQQ uptake |
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