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Figure 1.
Fig. 1. Structure of CysA: (a) Ribbon diagram of the CysA
monomer. The catalytic subdomain of the nucleotide-binding
domain is shown in purple, the helical subdomain in red, the
linker region in yellow and the regulatory domain in blue
(distal β-sandwich) and royal blue (proximal β-sandwich). The
location of conserved sequence motifs is indicated by capital
letters: ‘Walker’ sites (A, B), D-loop, Q-loop, ABC
signature (LSQ), and H motif. (b) Stereo representation of the
CysA-2 dimer found in an open state. The monomers were shown in
blue and red. For comparison CysA-2 was superimposed with the
MalK[eco](open) structure at the front side (red) and with the
MalK[eco](close) structure at the back side (green). In
addition, the regulatory domains of the CysA-1 monomers are
shown in yellow after superimposing with the catalytic domain.
Fig. 1 and Fig. 2 have the same orientation and were generated
using BOBSCRIPT [32].
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