Figure 1.
Figure 1. Schematic diagram of the NhaA structure. The core and dimer domains are illustrated with blue and beige shadowing, respectively. TM 4 (red) and TM 11 (yellow) are discontinuous and cross over in the center of the protein. Asp133 and Lys300 have been proposed to neutralize the positively and negatively charged helix dipoles of the discontinuous helices. Asp163 and Asp164 are thought to interact with the sodium ion. Coordinates are from Protein Data Bank accession number 1ZCD (Hunte et al., 2005).

Schematic diagram of the NhaA structure. The core and dimer domains are illustrated with blue and beige shadowing, respectively. TM 4 (red) and TM 11 (yellow) are discontinuous and cross over in the center of the protein. Asp133 and Lys300 have been proposed to neutralize the positively and negatively charged helix dipoles of the discontinuous helices. Asp163 and Asp164 are thought to interact with the sodium ion. Coordinates are from Protein Data Bank accession number 1ZCD (Hunte et al., 2005).

This Feature Is Available To Subscribers Only

or Create an Account

Close Modal
Close Modal