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Structural adaptation of a protein to increased metal stress: NMR structure of a marine snail metallothionein with an additional domain


Baumann, Christian; Beil, Andrea; Jurt, Simon; Niederwanger, Michael; Palacios, Oscar; Capdevila, Merce; Atrian, Silvia; Dallinger, Reinhard; Zerbe, Oliver (2017). Structural adaptation of a protein to increased metal stress: NMR structure of a marine snail metallothionein with an additional domain. Angewandte Chemie Internationale Edition, 129(16):4688-4693.

Abstract

In this study we present the NMR structure of the metallothionein (MT) from the snail Littorina littorea (LlMT) when complexed to 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 built in three individual domains, each folding into a single well-defined three-metal cluster. The center α2 and C-terminal β domains are in a unique relative orientation. Two variants with longer and shorter linkers were investigated, revealing that specific inter-domain 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 to Littorina littorea an evolutionary advantage in coping with Cd2+ stress and adverse environmental conditions.

Abstract

In this study we present the NMR structure of the metallothionein (MT) from the snail Littorina littorea (LlMT) when complexed to 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 built in three individual domains, each folding into a single well-defined three-metal cluster. The center α2 and C-terminal β domains are in a unique relative orientation. Two variants with longer and shorter linkers were investigated, revealing that specific inter-domain 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 to Littorina littorea an evolutionary advantage in coping with Cd2+ stress and adverse environmental conditions.

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Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:07 Faculty of Science > Department of Chemistry
Dewey Decimal Classification:540 Chemistry
Uncontrolled Keywords:Metallothionein metal cluster metalloprotein NMR Structural Biology
Date:2017
Deposited On:02 Mar 2017 13:55
Last Modified:24 Apr 2017 01:03
Publisher:Wiley-VCH Verlag
ISSN:1433-7851
Funders:Swiss National Science Foundation
Publisher DOI:https://doi.org/10.1002/ange.201611873

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