Correction to: Nature Structural & Molecular Biology https://doi.org/10.1038/s41594-019-0351-6, published online 23 December 2019.
In the version of the article initially published, the phospho-citryl-CoA intermediate in the ACLY-E599Q–ATP-citrate-CoA structure (PDB 6UUW) was modeled incorrectly. Specifically, the citryl-CoA linkage was modeled with a thioether bond instead of a thioester bond, and the phosphate group was connected to the -OH of the citryl moiety in the phospho-citryl portion rather than via an ester bond with the carboxylate group, as supported by Walsh and Spector (J. Biol. Chem. 243, 446–448, 1968). Thus, the intermediate shown in Fig. 6 and Extended Data Fig. 7c,d was incorrect. The PDB coordinate file has been revised and the original and corrected Fig. 6 and Extended Data Fig. 7c,d are given here. The text has not been altered to reflect these changes, but given the inherent instability of the modeled phospho-citryl-CoA intermediate and the limited resolution of the current structure, the modeled intermediate could represent phospho-citrate + CoA, citryl-CoA + phosphate or a mixture of the two. Given these possibilities, the precise catalytic role of E599 is unknown and E599 may not be directly involved in cleavage of the citryl-CoA adduct, as suggested in the article.
In addition, in Table 1, the number of ligand atoms in the “E599Q with ATP-citrate-CoA (D2)” structure was incorrectly listed as 4; the correct number is 8. Also in Table 1, the bond length r.m.s. deviation in the “With citrate-CoA (C1 assym. closed)” structure was incorrectly listed as 0.0008 Å; the correct value is 0.008 Å. The ACLY-E599Q mutant was incorrectly identified as ACLY-E599A in the following locations: in Results section “ACLY catalysis proceeds through a phospho-citryl-CoA intermediate in the ASH domain”, paragraph 16, phrase “We therefore mixed the ACLY-E559Q mutant with saturating concentrations ...”; in the Discussion, paragraph 17, phrase “Interestingly, citrate was added to both the ACLY–citrate-CoA and ACLY-E599Q–ATP-citrate-CoA structures ...”; and in the Discussion, paragraph 20, sentence “This conclusion is further supported by our ability to trap a phospho-citryl-CoA intermediate bound to ACLY-E599Q catalytic mutant.” In the Methods section “Cryo-EM data collection, image processing, model building and refinement”, paragraph 28, the mutated residue Q was excluded from the name of the mutant in the phrase “For 3D reconstruction of the ACLY-E599Q–citrate-ATP-CoA structure ....” In Extended Data Fig. 4b, incorrect residue ranges were given for helical segments from the CSH domain of ACLY: the residue range was labeled as “resi 1055-1088” in the left and right panels, and the figure caption gave it as “residues 1055-1080.” The correct residue range label is “resi 1055-1077” and the correct figure caption text is “Cryo-EM density of representative helical segments (residues 1055-1077) from ACLY–citrate-CoA (left) and ACLY–OAA–acetyl-CoA structures.” The errors have been corrected in the HTML and PDF versions of the article.
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
About this article
Cite this article
Wei, X., Schultz, K., Bazilevsky, G.A. et al. Author Correction: Molecular basis for acetyl-CoA production by ATP-citrate lyase. Nat Struct Mol Biol 27, 511–513 (2020). https://doi.org/10.1038/s41594-020-0421-9
Published:
Issue Date:
DOI: https://doi.org/10.1038/s41594-020-0421-9
This article is cited by
-
Reply to: Acetyl-CoA is produced by the citrate synthase homology module of ATP-citrate lyase
Nature Structural & Molecular Biology (2021)
-
Acetyl-CoA is produced by the citrate synthase homology module of ATP-citrate lyase
Nature Structural & Molecular Biology (2021)