5ml1
From Proteopedia
NMR Structure of the Littorina littorea metallothionein, a snail MT folding into three distinct domains
Structural highlights
FunctionPublication Abstract from PubMedIn 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 alpha2 and C-terminal beta 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 alpha1 and alpha2 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. Structural Adaptation of a Protein to Increased Metal Stress: NMR Structure of a Marine Snail Metallothionein with an Additional Domain.,Baumann C, Beil A, Jurt S, Niederwanger M, Palacios O, Capdevila M, Atrian S, Dallinger R, Zerbe O Angew Chem Int Ed Engl. 2017 Apr 10;56(16):4617-4622. doi:, 10.1002/anie.201611873. Epub 2017 Mar 23. PMID:28332759[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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