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TitleHigh-affinity PQQ import is widespread in Gram-negative bacteria.
Journal, issue, pagesSci Adv, Vol. 11, Issue 22, Page eadr2753, Year 2025
Publish dateMay 30, 2025
AuthorsFabian Munder / Marcos Voutsinos / Klaus Hantke / Hari Venugopal / Rhys Grinter /
PubMed AbstractPyrroloquinoline 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 linksSci Adv / PubMed:40446051 / PubMed Central
MethodsEM (single particle)
Resolution1.99 Å
Structure data

EMDB-45192, PDB-9c4o:
Cryo-EM structure of PqqU with ligand PQQ
Method: EM (single particle) / Resolution: 1.99 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-PQQ:
PYRROLOQUINOLINE QUINONE

ChemComp-HOH:
WATER

Source
  • escherichia coli bw25113 (bacteria)
KeywordsMEMBRANE PROTEIN / TonD-dependent / outer membrane / transporter / PQQ uptake

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