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. 2004 Jul 15;101(30):10937–10942. doi: 10.1073/pnas.0401742101

Fig. 3.

Fig. 3.

Domain movements in monomeric SecA. Ribbon diagram of monomeric B. subtilis SecA in the open conformation (a) and of a single subunit of dimeric B. subtilis SecA in the closed conformation (b). Color codes are as described for Fig. 1. The first and last helices in the PPXD are represented as cylinders to better visualize the transition between the conformations. The arrows in a indicate the movements that are required to convert the open conformation to the closed conformation. The side chains of residues 232 and 773 are shown in red in stick representation. Corresponding E. coli SecA residue numbers are given in parentheses. These residues were mutated to cysteines in E. coli SecA, and the accessibility of residue 824 to a modification reagent was used to probe the transition from the closed to the open conformation.