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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 2021 Sep 9;118(38):e2113619118. doi: 10.1073/pnas.2113619118

Correction for Li et al., Structure of the Dietzia Mrp complex reveals molecular mechanism of this giant bacterial sodium proton pump

PMCID: PMC8463799  PMID: 34503997

CELL BIOLOGY, CHEMISTRY Correction for “Structure of the Dietzia Mrp complex reveals molecular mechanism of this giant bacterial sodium proton pump,” by Bin Li, Kaiduan Zhang, Yong Nie, Xianping Wang, Yan Zhao, Xuejun C. Zhang, and Xiao-Lei Wu, which was first published November 23, 2020; 10.1073/pnas.2006276117 (Proc. Natl. Acad. Sci. U.S.A. 117, 31166–31176).

The authors note that the order of the affiliations was incorrect. The affiliation for College of Engineering, Peking University, 100871 Beijing, China, should have been listed as the first affiliation.

The authors also note that the following text should be added to the article as a Note Added in Proof:

Note Added in Proof. “We first submitted this manuscript on April 3, 2020. During review and production, an article, ‘Structure and mechanism of the Mrp complex, an ancient cation/proton antiporter,’ was submitted by Steiner and Sazanov in June 2020 and published in July 2020 (50). The article reported the structure of Group-I Mrp complex from Anoxybacillus flavithermus (AfMrp). However, in contrast to the six subunits in DqMrp analyzed in our group, the AfMrp complex contains seven subunits. Second, the AfMrp structure was determined in an elongated dimer form, with the MrpE subunit serving as the dimerization interface. Third, in the AfMrp complex, a highly negatively charged cavity is reported to be located between the MrpA and MrpF subunits; however, there is no significant cavity observed in corresponding position in our DqMrp complex. Our DqMrp complex seems to use a Na+-transport path distinct from the one proposed for AfMrp. To identify and verify amino acid residues critically involved in the mechanism responsible for salt resistance, we introduced a series of positions in potential proton/Na+ transport pathways. Further studies on both systems might help characterize the transition motion for all proteins in the family.”

The full citation for ref. 50 appears below. The online version has been corrected to include the above note and to add ref. 50 to the References list.

50. J. Steiner, L. Sazanov, Structure and mechanism of the Mrp complex, an ancient cation/proton antiporter. eLife 9, e59407 (2020).


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