8QJ4

Receptor Sd-Amt1 (ON-state)

8QJ4 の概要

• エントリーDOI: 10.2210/pdb8qj4/pdb
• 関連するPDBエントリー: 8QJ3
• 分子名称: Ammonium transporter, CHLORIDE ION, AMMONIUM ION, ... (4 entities in total)
• 機能のキーワード: ammonium receptor, on-state, shewanella denitrificans, sd-amt1, diguanylate cyclase, amt, signaling protein
• 由来する生物種: Shewanella denitrificans OS217
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 141887.06

構造登録者

Andrade, S.L.,Pflueger, T.,Gschell, M. (登録日: 2023-09-12, 公開日: 2024-06-12)

主引用文献

Pfluger, T.,Gschell, M.,Zhang, L.,Shnitsar, V.,Zabadne, A.J.,Zierep, P.,Gunther, S.,Einsle, O.,Andrade, S.L.A.
How sensor Amt-like proteins integrate ammonium signals.
Sci Adv, 10:eadm9441-eadm9441, 2024

PubMed Abstract: Unlike aquaporins or potassium channels, ammonium transporters (Amts) uniquely discriminate ammonium from potassium and water. This feature has certainly contributed to their repurposing as ammonium receptors during evolution. Here, we describe the ammonium receptor Sd-Amt1, where an Amt module connects to a cytoplasmic diguanylate cyclase transducer module via an HAMP domain. Structures of the protein with and without bound ammonium were determined to 1.7- and 1.9-Ångstrom resolution, depicting the ON and OFF states of the receptor and confirming the presence of a binding site for two ammonium cations that is pivotal for signal perception and receptor activation. The transducer domain was disordered in the crystals, and an AlphaFold2 prediction suggests that the helices linking both domains are flexible. While the sensor domain retains the trimeric fold formed by all Amt family members, the HAMP domains interact as pairs and serve to dimerize the transducer domain upon activation.

PubMed: 38838143
DOI: 10.1126/sciadv.adm9441

実験手法

X-RAY DIFFRACTION (1.7 Å)