Since the publication of this article, the authors have noticed several errors that in any case do not affect the original conclusions presented. The authors apologize for any inconvenience caused.
The gel presented in panel A of Figure 2 suggests a slightly incorrect size for the purified CYC domain of XC_250. Panel E in the same figure incorrectly describes D28 as D41 (see below). The correct figure and legend are shown below. Source data for this figure is now available on the online supplementary information page.
The predicted critical amino acid sites of XC_0250 were reported incorrectly in the section ‘The cyclase domain of XC_0250 is active in cyclic GMP synthesis’, with D28 described as D41. The text should have read:
‘The two critical metal‐ion binding aspartates are conserved (D28 and D71) as well as an alanine (A150) residue that occupies a substrate‐specifying position. However, the transition state‐stabilizing asparagine and arginine residues are substituted by leucine (L157) and alanine (A161). The importance of both conserved and altered residues (D28, D41, D71, L73, A150, L157, A161) for the enzymatic activity of this domain was examined by assessing the effects of alanine or serine substitutions’.
And at a later point in the same section: ‘Several of these residues (D28, D71, A150, L157) are conserved in the R. centenum guanylyl cyclase (Supplementary Fig S1).’
Consistent with this, the alignment in Supplementary Fig S1 panel A incorrectly shows the position of D28. The correct figure and legend are available above.
Supplementary Figure S1
Source Data for Suppl. Figure S1
- Copyright © 2013 European Molecular Biology Organization