Purification of NhaA Na+/H+ antiporter of Escherichia coli for 3D or 2D 
crystallization

Venturi, Miro; Padan, Etana

doi:10.1016/B978-012361776-7/50011-5

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Purification of NhaA Na⁺/H⁺ antiporter of Escherichia coli for 3D or 2D crystallization

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Venturi, Miro
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Venturi, M., & Padan, E. (2003). Purification of NhaA Na⁺/H⁺ antiporter of Escherichia coli for 3D or 2D crystallization. In C. Hunte, G. von Jagow, & H. Schägger (Eds.), Membrane Protein Purification and Crystallization (pp. 179-190). San Diego, CA, U.S.A.: Academic Press/Elsevier Science. doi:10.1016/B978-012361776-7/50011-5.

Cite as: http://hdl.handle.net/11858/00-001M-0000-0024-DB91-E

Abstract

INTRODUCTION NhaA, the Na⁺/H⁺ antiporter of Escherichia coli, is a polytopic membrane protein. These are very hydrophobic polypeptides that contain several putative transmembrane helices (TMS) connected by hydrophilic loops. Of the genomes sequenced so far, as many as 30% of the gene products are known or predicted to be polytopic transmembrane proteins. These proteins catalyze a multitude of essential functions; transport of molecules across membranes of cells and organelles is just one important function. Moreover, many transport proteins are important drug targets (e.g., Prozac), and an increasing number of human diseases are being traced to mutations in transport proteins (e.g., cystic fibrosis). Nevertheless, no atomic structure of any of these proteins has been solved.