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• W4224267826 abstract "SUMMARY The Na + -pumping NADH-ubiquinone oxidoreductase (Na + -NQR) couples electron transfer from NADH to ubiquinone with Na + -pumping, generating an electrochemical Na + gradient that is essential for energy-consuming reactions in bacteria. Since Na + -NQR is exclusively found in prokaryotes, it is a promising target for highly selective antibiotics. However, the molecular mechanism of inhibition is not well-understood for lack of the atomic structural information about an inhibitor-bound state. Here we present cryo-electron microscopy structures of Na + - NQR from Vibrio cholerae with or without a bound inhibitor at 2.5- to 3.1-Å resolution. The structures reveal the arrangement of all six redox cofactors including riboflavin, whose position has been under debate, and a newly assigned 2Fe-2S NqrD/E cluster located between the membrane embedded NqrD and NqrE subunits. A large part of the hydrophilic NqrF near the cytoplasmic membrane surface is barely visible in the density map, suggesting a high degree of flexibility. This flexibility may be responsible to reducing the long distance between the 2Fe- 2S centers in NqrF and NqrD/E, consistent with physiologically relevant electron transfer. Two different types of specific inhibitors (korormicin A and aurachin D-42) bind to the N-terminal region of NqrB, which is disordered in the absence of inhibitors. The current inhibitor-bound structures reasonably explain our previous biochemical findings obtained by different chemistry-based experiments. This study provides a definite foundation for understanding the function of Na + -NQR and the molecular mechanism of its specific inhibitors to support molecular design of new antibiotics targeting the enzyme." @default.
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• W4224267826 date "2022-04-19" @default.
• W4224267826 modified "2023-09-28" @default.
• W4224267826 title "Cryo-EM structures of Na⁺-pumping NADH-ubiquinone oxidoreductase from <i>Vibrio cholerae</i>" @default.
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• W4224267826 doi "https://doi.org/10.1101/2022.04.19.488743" @default.
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