5MN3

NMR structure of the Littorina littorea metallothionein, a snail MT folding into three distinct domains

5MN3 の概要

• エントリーDOI: 10.2210/pdb5mn3/pdb
• 関連するPDBエントリー: 5ML1
• NMR情報: BMRB: 34076
• 分子名称: domain-swapped metallothionein from Littorina Littorea, CADMIUM ION (2 entities in total)
• 機能のキーワード: nmr metallothionein metal cluster, metal transport
• 由来する生物種: Littorina litorea; 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11207.42

構造登録者

Zerbe, O.,Jurt, S.,Baumann, C. (登録日: 2016-12-12, 公開日: 2017-12-20, 最終更新日: 2025-12-17)

主引用文献

Baumann, C.,Beil, A.,Jurt, S.,Niederwanger, M.,Palacios, O.,Capdevila, M.,Atrian, S.,Dallinger, R.,Zerbe, O.
Structural Adaptation of a Protein to Increased Metal Stress: NMR Structure of a Marine Snail Metallothionein with an Additional Domain
Angew.Chem.Int.Ed.Engl., 56:4617-4622, 2017

PubMed Abstract: In this study, we present an NMR structure of the metallothionein (MT) from the snail Littorina littorea (LlMT) in complex with Cd . LlMT is capable of binding 9 Zn or 9 Cd 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 Cd stress and adverse environmental conditions.

PubMed: 28332759
DOI: 10.1002/anie.201611873

実験手法

SOLUTION NMR