4U4T

Structure of a nitrate/nitrite antiporter NarK in nitrate-bound inward-open state

4U4T の概要

• エントリーDOI: 10.2210/pdb4u4t/pdb
• 関連するPDBエントリー: 4U4V 4U4W
• 分子名称: Nitrate/nitrite transporter NarK, NITRATE ION, ZINC ION, ... (6 entities in total)
• 機能のキーワード: transporter, nitrate nitrite porter family, major facilitator superfamily, membrane transporter, transport protein
• 由来する生物種: Escherichia coli str. K12 substr. MG1655
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 53527.50

構造登録者

Fukuda, M.,Takeda, H.,Kato, H.E.,Doki, S.,Ito, K.,Maturana, A.D.,Ishitani, R.,Nureki, O. (登録日: 2014-07-24, 公開日: 2015-07-15, 最終更新日: 2024-03-20)

主引用文献

Fukuda, M.,Takeda, H.,Kato, H.E.,Doki, S.,Ito, K.,Maturana, A.D.,Ishitani, R.,Nureki, O.
Structural basis for dynamic mechanism of nitrate/nitrite antiport by NarK
Nat Commun, 6:7097-7097, 2015

PubMed 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.

PubMed: 25959928
DOI: 10.1038/ncomms8097

実験手法

X-RAY DIFFRACTION (2.4 Å)