Journal of Molecular Biology
Regular ArticleNMR Structure of the Sea Urchin (Strongylocentrotus purpuratus) Metallothionein MTA☆,☆☆
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Cited by (81)
Characterisation of the metallothionein gene in the Sydney rock oyster and its expression upon metal exposure in oysters with different prior metal exposure histories
2019, Marine Environmental ResearchCitation Excerpt :The unique feature of MTs is the arrangement of conserved Cys residues in the recurring structural motifs of Cys-Cys, Cys-X-Cys and Cys-X-X-Cys, which display a strong affinity to bind metal ions (X stands herein for any amino acid except Cys; Hamer, 1986) through the formation of metal-thiolate bonds. The number of Cys residues determines the two types of MT domains, α and β, which are able to bind metals independently and are joined by a short linker region (Braun et al., 1992; Riek et al., 1999). The α domain, typically possessing 11–12 Cys residues, binds 4 divalent metal ions whereas the β domain, typically possessing 9 Cys residues, binds 3 divalent metal ions.
Complexation of the Zn, Co, Cd, and Pb ions by metallothioneins: A QM/MM simulation
2017, Computational and Theoretical ChemistryThe sea urchin metallothionein system: Comparative evaluation of the SpMTA and SpMTB metal-binding preferences
2013, FEBS Open BioCitation Excerpt :The SpMTA cDNA was kindly provided by Prof. Kägi and subsequently cloned into the pGEX-4T1 BamHI/SalI restriction sites added by PCR amplification, using 5′-CCCGGATCCATGCCTGATGTCAAG-3′ as upstream primer and 5′-GCGCCCGTCGACCTAGCATGCACA-3′ as downstream primer. According to the reported SpMTA domain boundaries [15], cDNAs encoding for its separate moieties were obtained by PCR reactions that added BamHI/XhoI restriction sites with the following oligonucleotides: for the N-terminal fragment or α domain (encompassing residues 1–36 of the full polypeptide), 5′-CCCGGATCCATGCCTGATGTCAAG-3′ (upstream) and 5′-AAACTCGAGTCATCCACAGCAGGTTCCATCCTTG-3′ (downstream); and for the C-terminal fragment or β domain (residues 37–64 of the full polypeptide), 5′-ACACACGGATCCATATGCACAAACGCTGCATGC-3′ (upstream) and 5′-AAACCCCTCGAGCTAGCATGCACAGTTCCCCTC-3′ (downstream). The cDNA of the SpMTB isoform was obtained from the Sea Urchin Genome Project Library Collection, in the California Institute of Technology (Caltech), and corresponded to the EST clone PMC_62379562 (seq ID NCBI 214576).
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Abbreviations used: MT, metallothionein; MTA, MT isoform A of Strongylocentrotus purpuratus; MTAα, α-domain of MTA; MTAβ, β-domain of MTA; hMT-2, human MT isoform 2; MT-2α, α-domain of MT-2; MT-2β, β-domain of MT-2; MT-1, lobster or blue crab MT isoform 1; MT-1α, α-domain of MT-1; MT-1β, β-domain of MT-1; NMR, nuclear magnetic resonance; NOE, nuclear Overhauser effect; 2D, two-dimensional; NOESY, NOE spectroscopy; COSY, correlation spectroscopy; TOCSY, total correlation spectroscopy; ppm, parts per million; 3JHNα, vicinal spin-spin coupling constant between the backbone amide proton and the α-proton; 3Jαβ, vicinal spin-spin coupling constant between the α-proton and one of the β-protons; r.m.s.d., root-mean-square deviation
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Edited by P. E. Wright
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Present addresses: Dr Yunyuan Wang, Department of Medical Biochemistry, Texas A&M University Health Science Center, College of Medicine, 440 Reynolds Medical Bldg., College Station, TX 77843-1114, USA; Dr Elaine A. Mackay, 1 Caswall Close, Foxley Field, Binfield, Berkshire RG42 4EF, UK
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Corresponding author