Structural basis for dynamic mechanism of nitrate/nitrite antiport by NarK

Masahiro Fukuda, Hironori Takeda, Hideaki E. Kato, Shintaro Doki, Koichi Ito, Andrés D. Maturana, Ryuichiro Ishitani () and Osamu Nureki ()
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Masahiro Fukuda: Graduate School of Science, The University of Tokyo
Hironori Takeda: Graduate School of Science, The University of Tokyo
Hideaki E. Kato: Graduate School of Science, The University of Tokyo
Shintaro Doki: Graduate School of Science, The University of Tokyo
Koichi Ito: Graduate School of Frontier Sciences, The University of Tokyo
Andrés D. Maturana: Graduate School of Bioagricultural Sciences, Nagoya University, Furo-cho
Ryuichiro Ishitani: Graduate School of Science, The University of Tokyo
Osamu Nureki: Graduate School of Science, The University of Tokyo

Nature Communications, 2015, vol. 6, issue 1, 1-12

Abstract: Abstract NarK belongs to the nitrate/nitrite porter (NNP) family in the major facilitator superfamily (MFS) and plays a central role in nitrate uptake across the membrane in diverse organisms, including archaea, bacteria, fungi and plants. Although previous studies provided insight into the overall structure and the substrate recognition of NarK, its molecular mechanism, including the driving force for nitrate transport, remained elusive. Here we demonstrate that NarK is a nitrate/nitrite antiporter, using an in vitro reconstituted system. Furthermore, we present the high-resolution crystal structures of NarK from Escherichia coli in the nitrate-bound occluded, nitrate-bound inward-open and apo inward-open states. The integrated structural, functional and computational analyses reveal the nitrate/nitrite antiport mechanism of NarK, in which substrate recognition is coupled to the transport cycle by the concomitant movement of the transmembrane helices and the key tyrosine and arginine residues in the substrate-binding site.

Date: 2015
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DOI: 10.1038/ncomms8097

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