5i32

Ammonia permeable aquaporin AtTIP2;1

spinqualitylabelsall models 5i32, resolution 1.18Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5i32 is a 1 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.18Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TIP21_ARATH Aquaporin required to facilitate the transport of water from the vacuolar compartment to the cytoplasm. Does not promote glycerol permability. Its function is impaired by Hg(2+). Transports urea in yeast cells and Xenopus laevis oocytes in a pH-independent manner. Transports methylammonium or ammonium in yeast cells and Xenopus laevis oocytes, preferentially at high medium pH. May participate in vacuolar compartmentation and detoxification of ammonium. Publication Abstract from PubMed Aquaporins of the TIP subfamily (Tonoplast Intrinsic Proteins) have been suggested to facilitate permeation of water and ammonia across the vacuolar membrane of plants, allowing the vacuole to efficiently sequester ammonium ions and counteract cytosolic fluctuations of ammonia. Here, we report the structure determined at 1.18 A resolution from twinned crystals of Arabidopsis thaliana aquaporin AtTIP2;1 and confirm water and ammonia permeability of the purified protein reconstituted in proteoliposomes as further substantiated by molecular dynamics simulations. The structure of AtTIP2;1 reveals an extended selectivity filter with the conserved arginine of the filter adopting a unique unpredicted position. The relatively wide pore and the polar nature of the selectivity filter clarify the ammonia permeability. By mutational studies, we show that the identified determinants in the extended selectivity filter region are sufficient to convert a strictly water-specific human aquaporin into an AtTIP2;1-like ammonia channel. A flexible histidine and a novel water-filled side pore are speculated to deprotonate ammonium ions, thereby possibly increasing permeation of ammonia. The molecular understanding of how aquaporins facilitate ammonia flux across membranes could potentially be used to modulate ammonia losses over the plasma membrane to the atmosphere, e.g., during photorespiration, and thereby to modify the nitrogen use efficiency of plants. Crystal Structure of an Ammonia-Permeable Aquaporin.,Kirscht A, Kaptan SS, Bienert GP, Chaumont F, Nissen P, de Groot BL, Kjellbom P, Gourdon P, Johanson U PLoS Biol. 2016 Mar 30;14(3):e1002411. doi: 10.1371/journal.pbio.1002411., eCollection 2016 Mar. PMID:27028365 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Aquaporin 3D structures

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