Structure of a prokaryotic virtual proton pump at 3.2|[thinsp]||[Aring]| resolution Export

@article{citeulike:5103480, abstract = {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 biochemistry1, 2, 3, 4, 5, 6, 7. 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'8 in the inner membrane, called AdiC3, 4, that imports l-arginine from the gastric juice and exports its decarboxylation product agmatine. AdiC belongs to the APC superfamily of membrane proteins6, 7, 9, which transports amino acids, polyamines and organic cations in a multitude of biological roles, including delivery of arginine for nitric oxide synthesis10, facilitation of insulin release from pancreatic -cells11, and, when inappropriately overexpressed, provisioning of certain fast-growing neoplastic cells with amino acids12, 13. High-resolution structures and detailed transport mechanisms of APC transporters are currently unknown. Here we describe a crystal structure of AdiC at 3.2 \r{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.}, author = {Fang, Yiling and Jayaram, Hariharan and Shane, Tania and Kolmakova-Partensky, Ludmila and Wu, Fang and Williams, Carole and Xiong, Yong and Miller, Christopher}, citeulike-article-id = {5103480}, citeulike-linkout-0 = {http://dx.doi.org/10.1038/nature08201}, citeulike-linkout-1 = {http://dx.doi.org/10.1038/nature08201}, day = {05}, doi = {10.1038/nature08201}, issn = {0028-0836}, journal = {Nature}, keywords = {imp, ms-13, structure}, month = {July}, number = {7258}, pages = {1040--1043}, posted-at = {2009-11-06 22:30:55}, priority = {2}, publisher = {Nature Publishing Group}, title = {Structure of a prokaryotic virtual proton pump at 3.2|[thinsp]||[Aring]| resolution}, url = {http://dx.doi.org/10.1038/nature08201}, volume = {460}, year = {2009} }

TY - JOUR ID - citeulike:5103480 L3 - citeulike-article-id:5103480 N2 - 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 biochemistry1, 2, 3, 4, 5, 6, 7. 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'8 in the inner membrane, called AdiC3, 4, that imports l-arginine from the gastric juice and exports its decarboxylation product agmatine. AdiC belongs to the APC superfamily of membrane proteins6, 7, 9, which transports amino acids, polyamines and organic cations in a multitude of biological roles, including delivery of arginine for nitric oxide synthesis10, facilitation of insulin release from pancreatic -cells11, and, when inappropriately overexpressed, provisioning of certain fast-growing neoplastic cells with amino acids12, 13. High-resolution structures and detailed transport mechanisms of APC transporters are currently unknown. Here we describe a crystal structure of AdiC at 3.2 Å 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. IS - 7258 JF - Nature SN - 0028-0836 EP - 1043 TI - Structure of a prokaryotic virtual proton pump at 3.2|[thinsp]||[Aring]| resolution PB - Nature Publishing Group VL - 460 SP - 1040 KW - imp KW - ms-13 KW - structure AU - Fang, Yiling AU - Jayaram, Hariharan AU - Shane, Tania AU - Kolmakova-Partensky, Ludmila AU - Wu, Fang AU - Williams, Carole AU - Xiong, Yong AU - Miller, Christopher PY - 2009/07/05/ UR - http://dx.doi.org/10.1038/nature08201 ER -