Structural Adaptation of a Protein to Increased Metal Stress: NMR Structure of a Marine Snail Metallothionein with an Additional Domain

Christian Baumann, Andrea Beil, Simon Jurt, Michael Niederwanger, Oscar Palacios, Mercè Capdevila, Sílvia Atrian, Reinhard Dallinger, Oliver Zerbe

Research output: Contribution to journalArticleResearchpeer-review

16 Citations (Scopus)

Abstract

© 2017 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim In this study, we present an NMR structure of the metallothionein (MT) from the snail Littorina littorea (LlMT) in complex with Cd2+. LlMT is capable of binding 9 Zn2+ or 9 Cd2+ ions. Sequence alignments with other snail MTs revealed that the protein is likely composed of three domains. The study revealed that the protein is divided into three individual domains, each of which folds into a single well-defined three-metal cluster. The central α2 and C-terminal β domains are positioned with a unique relative orientation. Two variants with longer and shorter linkers were investigated, which revealed that specific interdomain contacts only occurred with the wild-type linker. Moreover, a domain-swap mutant in which the highly similar α1 and α2 domains were exchanged was structurally almost identical. It is suggested that the expression of a three-domain MT confers an evolutionary advantage on Littorina littorea in terms of coping with Cd2+ stress and adverse environmental conditions.
Original languageEnglish
Pages (from-to)4617-4622
JournalAngewandte Chemie - International Edition
Volume56
Issue number16
DOIs
Publication statusPublished - 1 Jan 2017

Keywords

  • evolution
  • metal clusters
  • metallothionein
  • NMR
  • protein structures

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