Figure 2.
Fig. 2. Disulfide bridge and sulfate binding sites of
oxidized Spx. (A) The disulfide bridge is shown as yellow
sticks. The sulfate, which is found in both Spx and ArsC, and
may be involved in transcription regulation by Spx, is bound by
the guanidinium moiety of residue R92 and the main chain
carbonyl oxygen of S12. A second sulfate ion, which is found
only in the Spx- CTD structure, is shown
to the left of R92. Interactions between the sulfates and
protein are depicted by dashed line. (B) A representative 2F[o]
- F[c] simulated annealing composite omit map contoured at 1
shows the electron
density for the disulfide bridge of Spx.
CTD structure, is shown
to the left of R92. Interactions between the sulfates and
protein are depicted by dashed line. (B) A representative 2F[o]
- F[c] simulated annealing composite omit map contoured at 1
shows the electron
density for the disulfide bridge of Spx.