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


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2015-12

AUTHORS

Masahiro Fukuda, Hironori Takeda, Hideaki E. Kato, Shintaro Doki, Koichi Ito, Andrés D. Maturana, Ryuichiro Ishitani, Osamu Nureki

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. More... »

PAGES

7097

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/ncomms8097

DOI

http://dx.doi.org/10.1038/ncomms8097

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1002627513

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/25959928


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