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TitleProton-coupled transport mechanism of the efflux pump NorA.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 4494, Year 2024
Publish dateMay 27, 2024
AuthorsJianping Li / Yan Li / Akiko Koide / Huihui Kuang / Victor J Torres / Shohei Koide / Da-Neng Wang / Nathaniel J Traaseth /
PubMed AbstractEfflux pump antiporters confer drug resistance to bacteria by coupling proton import with the expulsion of antibiotics from the cytoplasm. Despite efforts there remains a lack of understanding as to ...Efflux pump antiporters confer drug resistance to bacteria by coupling proton import with the expulsion of antibiotics from the cytoplasm. Despite efforts there remains a lack of understanding as to how acid/base chemistry drives drug efflux. Here, we uncover the proton-coupling mechanism of the Staphylococcus aureus efflux pump NorA by elucidating structures in various protonation states of two essential acidic residues using cryo-EM. Protonation of Glu222 and Asp307 within the C-terminal domain stabilized the inward-occluded conformation by forming hydrogen bonds between the acidic residues and a single helix within the N-terminal domain responsible for occluding the substrate binding pocket. Remarkably, deprotonation of both Glu222 and Asp307 is needed to release interdomain tethering interactions, leading to opening of the pocket for antibiotic entry. Hence, the two acidic residues serve as a "belt and suspenders" protection mechanism to prevent simultaneous binding of protons and drug that enforce NorA coupling stoichiometry and confer antibiotic resistance.
External linksNat Commun / PubMed:38802368 / PubMed Central
MethodsEM (single particle)
Resolution3.26 - 3.61 Å
Structure data

41605

8tte

EMDB-41605, PDB-8tte:
Protonated state of NorA at pH 5.0
Method: EM (single particle) / Resolution: 3.26 Å

41606

8ttf

EMDB-41606, PDB-8ttf:
NorA double mutant - E222QD307N at pH 7.5
Method: EM (single particle) / Resolution: 3.61 Å

41607

8ttg

EMDB-41607, PDB-8ttg:
NorA single mutant - E222Q at pH 7.5
Method: EM (single particle) / Resolution: 3.35 Å

41608

8tth

EMDB-41608, PDB-8tth:
NorA single mutant - D307N at pH 7.5
Method: EM (single particle) / Resolution: 3.54 Å

Source
  • staphylococcus aureus (bacteria)
  • homo sapiens (human)
KeywordsTRANSPORT PROTEIN / Protonated NorA / efflux pump / MRSA / TRANSPORT PROTEIN/IMMUNE SYSTEM / E222QD307N NorA / TRANSPORT PROTEIN-IMMUNE SYSTEM complex / E222Q NorA / D307N NorA

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