Literature DB >> 31745241

Author Correction: Structure of full-length wild-type human phenylalanine hydroxylase by small angle X-ray scattering reveals substrate-induced conformational stability.

Catarina S Tomé1,2, Raquel R Lopes3, Pedro M F Sousa2, Mariana P Amaro3,4, João Leandro3,4, Haydyn D T Mertens5, Paula Leandro6, João B Vicente7.   

Abstract

An amendment to this paper has been published and can be accessed via a link at the top of the paper.

Entities:  

Year:  2019        PMID: 31745241      PMCID: PMC6863894          DOI: 10.1038/s41598-019-54425-2

Source DB:  PubMed          Journal:  Sci Rep        ISSN: 2045-2322            Impact factor:   4.379


Correction to: Scientific Reports 10.1038/s41598-019-49944-x, published online 20 September 2019 The authors would like to acknowledge the missing reference of Arturo and colleagues publication in the original version of the Article, which describes structural data for a full-length p.C29S PAH variant in its l-Phe-activated form. This paper is cited here as Ref. 1 and should have been included in the text as below. In the Introduction, the paragraph, “Structural analyses of hPAH have relied on crystal structures of truncated forms of the enzyme lacking one or two domains5–12 and full-length bound to BH412, and on crystallographic and SAXS structures of the full-length rat homologue13–15.” should read: “Structural analyses of hPAH have relied on crystal structures of truncated forms of the enzyme lacking one or two domains5–12 and full-length bound to BH412, and on crystallographic and SAXS structures of the full-length C29S variant form of hPAH1 and full-length rat homologue13–15.” In the same section, the paragraph, “Solution structural analyses of rat PAH confirmed distinct conformations for the inactive and l-Phe-activated enzymes and supported dimerisation of regulatory domains as the substrate activation mechanism13,15.” should read “Solution structural analyses of rat PAH and hPAH C29S variant confirmed distinct conformations for the inactive and l-Phe-activated enzymes and supported dimerisation of regulatory domains as the substrate activation mechanism1,13,15.” In the Discussion, “Similar variations in the 0.05–0.2 Å–1 region have previously been observed for rat PAH13,15.” should read: “Similar variations in the 0.05–0.2 Å–1 region have previously been observed for rat PAH13,15 and, more recently, for the hPAH C29S variant[1].” This correction does not alter the main conclusions of the Article.
  1 in total

1.  Biophysical characterization of full-length human phenylalanine hydroxylase provides a deeper understanding of its quaternary structure equilibrium.

Authors:  Emilia C Arturo; Kushol Gupta; Michael R Hansen; Elias Borne; Eileen K Jaffe
Journal:  J Biol Chem       Date:  2019-05-10       Impact factor: 5.157

  1 in total

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