8qpf

Ammonium Transporter Amt1 from Shewanella denitrificans

spinqualitylabelsall models 8qpf, resolution 2.53Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8qpf is a 3 chain structure with sequence from Shewanella denitrificans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2.53Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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-Angstrom 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. How sensor Amt-like proteins integrate ammonium signals.,Pfluger T, Gschell M, Zhang L, Shnitsar V, Zabadne AJ, Zierep P, Gunther S, Einsle O, Andrade SLA Sci Adv. 2024 Jun 7;10(23):eadm9441. doi: 10.1126/sciadv.adm9441. Epub 2024 Jun , 5. PMID:38838143 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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