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Figure 1.
Figure 1. Dimeric structure of B. subtilis SecA. (a)
Dimerization of SecA occurs at the prominent groove formed by
nbd2 and the ppx domain. Chain a is in gray and chain b is
color-coded for the individual domains of SecA. (b) Dimer
interface of chain a and b: residues 551 to 554 of subunit a
form a novel parallel β-sheet with the highly conserved region
connecting nbd1 to the ppx domain (residues 221 to 224). (c) The
equivalent dimer interface of chain b and a: the α-helical
conformation of residues 552 to 559 of chain b is seen in all
previously determined SecA structures. All Figures were
generated using Pymol [http://pymol.sourceforge.net/].
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