The Journal of General Physiology
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Published online 11 November 2002 doi:10.1085/jgp.20028699
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© Rockefeller University Press, 0022-1295/2002/12/845/ $5.00
Journal of General Physiology, Volume 120, Number 6, December 2002 845-853
The Cation Selectivity Filter of the Bacterial Sodium Channel, NaChBac

Lixia Yue, Betsy Navarro, Dejian Ren, Arnolt Ramos and David E. Clapham

Howard Hughes Medical Institute, Children's Hospital, Boston, MA 02115

Address correspondence to David E. Clapham, HHMI, Children's Hospital, 1309 Enders Bldg., 320 Longwood Ave., Boston, MA 02115. Fax: (617) 731-0787; E-mail: clapham{at}enders.tch.harvard.edu

The Bacillus halodurans voltage-gated sodium-selective channel (NaChBac) (Ren, D., B. Navarro, H. Xu, L. Yue, Q. Shi, and D.E. Clapham. 2001b. Science. 294:2372–2375), is an ideal candidate for high resolution structural studies because it can be expressed in mammalian cells and its functional properties studied in detail. It has the added advantage of being a single six transmembrane (6TM) orthologue of a single repeat of mammalian voltage-gated Ca2+ (CaV) and Na+ (NaV) channels. Here we report that six amino acids in the pore domain (LESWAS) participate in the selectivity filter. Replacing the amino acid residues adjacent to glutamatic acid (E) by a negatively charged aspartate (D; LEDWAS) converted the Na+-selective NaChBac to a Ca2+- and Na+-permeant channel. When additional aspartates were incorporated (LDDWAD), the mutant channel resulted in a highly expressing voltage-gated Ca2+-selective conductance.

Key Words: bacterial channels • calcium channels • sodium channels • ion/membrane channel


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