3ncy | pdb_00003ncy

X-ray crystal structure of an arginine agmatine antiporter (AdiC) in complex with a Fab fragment

spinqualitylabelsall models 3ncy, resolution 3.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3ncy is a 8 chain structure with sequence from "bacillus_typhimurium"_loeffler_1892 "bacillus typhimurium" loeffler 1892 and Lk3 transgenic mice. This structure supersedes the now removed PDB entry 3hqk. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: ADIC_SALTY ("Bacillus typhimurium" Loeffler 1892) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [ADIC_SALTY] Major component of the acid-resistance (AR) system allowing enteric pathogens to survive the acidic environment in the stomach. Exchanges extracellular arginine for its intracellular decarboxylation product agmatine (Agm) thereby expelling intracellular protons. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed To reach the mammalian gut, enteric bacteria must pass through the stomach. Many such organisms survive exposure to the harsh gastric environment (pH 1.5-4) by mounting extreme acid-resistance responses, one of which, the arginine-dependent system of Escherichia coli, has been studied at levels of cellular physiology, molecular genetics and protein biochemistry. This multiprotein system keeps the cytoplasm above pH 5 during acid challenge by continually pumping protons out of the cell using the free energy of arginine decarboxylation. At the heart of the process is a 'virtual proton pump' in the inner membrane, called AdiC, that imports L-arginine from the gastric juice and exports its decarboxylation product agmatine. AdiC belongs to the APC superfamily of membrane proteins, which transports amino acids, polyamines and organic cations in a multitude of biological roles, including delivery of arginine for nitric oxide synthesis, facilitation of insulin release from pancreatic beta-cells, and, when inappropriately overexpressed, provisioning of certain fast-growing neoplastic cells with amino acids. High-resolution structures and detailed transport mechanisms of APC transporters are currently unknown. Here we describe a crystal structure of AdiC at 3.2 A resolution. The protein is captured in an outward-open, substrate-free conformation with transmembrane architecture remarkably similar to that seen in four other families of apparently unrelated transport proteins. Structure of a prokaryotic virtual proton pump at 3.2 A resolution.,Fang Y, Jayaram H, Shane T, Kolmakova-Partensky L, Wu F, Williams C, Xiong Y, Miller C Nature. 2009 Aug 20;460(7258):1040-3. Epub 2009 Jul 5. PMID:19578361 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Monoclonal Antibodies 3D structures

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