Open Access

Erratum: Adaptive evolution in the toxicity of a spider’s venom enzymes

  • Aurélio Pedroso1,
  • Sergio Russo Matioli2,
  • Mario Tyago Murakami3,
  • Giselle Pidde-Queiroz1 and
  • Denise V. Tambourgi1Email author
BMC Evolutionary BiologyBMC series – open, inclusive and trusted201616:58

https://doi.org/10.1186/s12862-016-0623-2

Published: 7 March 2016

The original article was published in BMC Evolutionary Biology 2015 15:290

The original version of this article [1] was unfortunately published with a mistake. The figure legends for Figs. 8 and 9 were interchanged. The correct Figures and their associated legends are provided below:
Fig. 8

Electrostatic surface charge distribution of Class I and II SMases D highlighting the catalytic interface. The ellipses indicate the active-site pocket. a Class I; b Class II

Fig. 9

Structural interpretation of the positively selected sites. a Cartoon representation of the structural comparison between Class I and II SMases D. The fully conserved catalytic histidines (H12 and H47) and the three acidic residues (E32, D34 and D91) involved in the metal ion coordination are shown as sticks, with carbon atoms in green. The seven positively selected sites are shown as sticks and balls, with carbon atoms in yellow. The residues depicted in the positive sites correspond to those of SMase I from L. laeta, and the sequence numbering is also based on this molecule according to PDB entry 1XX1 (Murakami et al., 2005). The cartoon representation is coloured according to the secondary structure elements and the flexible loop F related to the second S-S bond found uniquely in Class II members (in orange, Class I; in red, Class II). The variable loop E is cyan and blue for Classes I and II, respectively. b Schematic representation of a Class I SMase D highlighting all of the positively selected sites for this class using the same colour pattern

Figure 8 Electrostatic surface charge distribution of Class I and II SMases D highlighting the catalytic interface. The ellipses indicate the active-site pocket. a Class I; b Class II.

Figure 9 Structural interpretation of the positively selected sites. a Cartoon representation of the structural comparison between Class I and II SMases D. The fully conserved catalytic histidines (H12 and H47) and the three acidic residues (E32, D34 and D91) involved in the metal ion coordination are shown as sticks, with carbon atoms in green. The seven positively selected sites are shown as sticks and balls, with carbon atoms in yellow. The residues depicted in the positive sites correspond to those of SMase I from L. laeta, and the sequence numbering is also based on this molecule according to PDB entry 1XX1 (Murakami et al., 2005). The cartoon representation is coloured according to the secondary structure elements and the flexible loop F related to the second S-S bond found uniquely in Class II members (in orange, Class I; in red, Class II). The variable loop E is cyan and blue for Classes I and II, respectively. b Schematic representation of a Class I SMase D highlighting all of the positively selected sites for this class using the same colour pattern.

Notes

Declarations

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

Authors’ Affiliations

(1)
Laboratório de Imunoquímica, Instituto Butantan
(2)
Departamento de Genética e Biologia Evolutiva, Instituto de Biociências, Universidade de São Paulo
(3)
Laboratório Nacional de Biociências, Centro Nacional de Pesquisa em Energia e Materiais

Reference

  1. Pedroso A, Matioli SR, Murakami MT, Pidde-Queiroz G, Tambourgi DV. BMC Evol Biol. 2015;15:290. doi:10.1186/s12862-015-0561-4.View ArticlePubMedPubMed CentralGoogle Scholar

Copyright

© Pedroso et al. 2016

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