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Correction

Correction: Escherichia coli DnaE Polymerase Couples Pyrophosphatase Activity to DNA Replication

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Fig 3 is incorrect. The authors have provided a corrected version here. The publisher apologizes for the error.

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Fig 3. Structures of E. coli PHP and type-II inorganic PPases.

A) Tertiary structure of E. coli DNA Polymerase III α subunit (PDB 2HNH). The PHP and the Polymerase domains are represented in green and blue, respectively. B,C) Detail of the entire PHP domain (B) and of the PHP β-sheet (C). The antiparallel β-strand is represented in C with green colour. D,E) Active sites of the type-II inorganic PPase from Bacillus subtilis (D, PDB 1WPM) and Streptococcus gordonii (E, PDB 1K20). The proposed active site of E. coli PHP is shown in panel F. The following amino acids are shown as sticks: H9, D13, D15, D75, H98, and D149 (D, Bacillus subtilis); H9, D13, D15, D77, H99, and D151 (E, Streptococcus gordonii); H12, D19, D43, D69, H83, and D201 (F, Escherichia coli PHP).

https://doi.org/10.1371/journal.pone.0157207.g001

Reference

  1. 1. Lapenta F, Montón Silva A, Brandimarti R, Lanzi M, Gratani FL, Vellosillo Gonzalez P, et al. (2016) Escherichia coli DnaE Polymerase Couples Pyrophosphatase Activity to DNA Replication. PLoS ONE 11(4): e0152915. pmid:27050298

Citation: The PLOS ONE Staff (2016) Correction: Escherichia coli DnaE Polymerase Couples Pyrophosphatase Activity to DNA Replication. PLoS ONE 11(6): e0157207. https://doi.org/10.1371/journal.pone.0157207

Published: June 6, 2016

Copyright: © 2016 The PLOS ONE Staff. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.