NMR Structure of the Sea Urchin (Strongylocentrotus purpuratus) Metallothionein MTA

Riek, R. F.; Prêcheur, Bénédicte; Wang, Yunyuan; Mackay, Elaine A.; Wider, Gerhard; Güntert, Peter; Liu, Aizhuo; Kägi, Jeremias H. R.; Wüthrich, Kurt

doi:10.1006/jmbi.1999.2967

Cited by 87 publications

(71 citation statements)

References 49 publications

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“…Two basic metal-thiolate structures are known: The M II 4 Cys 11 cluster of the -domain of vertebrate and echinoderm MTs [15][16][17][18][19][20][21][22][23] and the M II 3 Cys 9 cluster of the -domain of vertebrate, crustacean, and echinoderm MTs (Fig. 2) [15][16][17][20][21][22][23][24][25]. Fig.…”

Section: Metal Ion Contentsmentioning

confidence: 99%

Structural features specific to plant metallothioneins

Freisinger

2011

J Biol Inorg Chem

112

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The metallothionein (MT) superfamily combines a large variety of small cysteine-rich proteins from nearly all phyla of life that have the ability to coordinate various transition metal ions, including Zn(II), Cd(II), and Cu(I). The members of the plant MT family are characterized by great sequence diversity, requiring further subdivision into four subfamilies. Very peculiar and not well understood is the presence of rather long cysteine-free amino acid linkers between the cysteine-rich regions. In light of the distinct differences in sequence to MTs from other families, it seems obvious to assume that these differences will also be manifested on the structural level. This was already impressively demonstrated with the elucidation of the three-dimensional structure of the wheat E(c)-1 MT, which revealed two metal cluster arrangements previously unprecedented for any MT. However, as this structure is so far the only one available for the plant MT family, other sources of information are in high demand. In this review the focus is thus set on any structural features known, deduced, or assumed for the plant MT proteins. This includes the determination of secondary structural elements by circular dichroism, IR, and Raman spectroscopy, the analysis of the influence of the long linker regions, and the evaluation of the spatial arrangement of the sequence separated cysteine-rich regions with the aid of, e.g., limited proteolytic digestion. In addition, special attention is paid to the contents of divalent metal ions as the metal ion to cysteine ratios are important for predicting and understanding possible metal-thiolate cluster structures. Very peculiar and not well understood is the presence of rather long Cys-free amino acid linkers between the Cys-rich regions. In light of the distinct differences in sequence to MTs from other families it seems obvious to assume that these differences will be also manifested on the structural level. This was already impressively demonstrated with the elucidation of the three-dimensional structure of the wheat E c -1 MT, which revealed two metal cluster arrangements previously unprecedented for any MT. However, as this structure is so far the only one available for the plant MT family other sources of information are of high demand.In this review the focus is thus set on any structural features known, deduced or assumed for the plant MT proteins. This includes the determination of secondary structural elements by CD, IR, and Raman spectroscopy, the analysis of the influence of the long linker regions, as well as the evaluation of the spatial arrangement of the sequence separated Cys-rich regions with the aid of e.g. limited proteolytic digestion. In addition, special attention is paid to the contents of divalent metal ions as the metal ion-to-Cys ratios are important for predicting and

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Section: Metal Ion Contentsmentioning

confidence: 99%

Structural features specific to plant metallothioneins

Freisinger

2011

J Biol Inorg Chem

112

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“…3B,C). [18,[22][23][24] Clusters with four divalent metal ions, M II 4 Cys 11 or M II 4 Cys 9 His 2 , are called aclusters and are part of vertebrate, echinodermata, as well as cyanobacterial MTs (Fig. 3D,E).…”

Section: Three-dimensional Structures Of Metal-thiolate Clustersmentioning

confidence: 99%

“…3D,E). [18,24,25] Cyanobacterial Zn 4 SmtA was the first structure of a MT that revealed partici pation of histidine (His) residues in the coordination of metal ions. The only known structure of a metalthiolate clus ter with monovalent metal ions is the one of the Cu I specific MT CUP1 from yeast (Fig.…”

Section: Three-dimensional Structures Of Metal-thiolate Clustersmentioning

confidence: 99%

The Metal-Thiolate Clusters of Plant Metallothioneins

Freisinger

2010

Chimia

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While structures of mammalian metallothioneins and their metal-thiolate clusters have been known for nearly 20 years, the first three-dimensional structure of a plant metallothionein was only published very recently. Also in other aspects, research on plant metallothioneins lags behind what is known about the vertebrate forms. However, in the past years more and more information, mostly based on experiments performed with optical spectroscopy has become available and permit sometimes unforeseen insights. In the following, the different experimental strategies applied in our laboratory will be described together with the progress we have made over the past years in detecting and characterizing the metal-thiolate clusters of plant metallothioneins.

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“…The three-metal cluster is located in the N-terminal b-domain and the four metal clusters in the C-terminal a-domain (Braun et al, 1992;Robbins et al, 1991;Dabrio et al, 2002). The other liquid phase NMR structures are those of equinoderme (Riek et al, 1999) and crab (Narula et al, 1995). Both structures revealed a monomeric protein composed of two globular domains binding a four-and a three-metal cluster in the equinodermal MT and two three metalclusters in the crustacean MT.…”

Section: Introductionmentioning

confidence: 99%

Isolation and characterisation of metallothionein from the clam Ruditapes decussatus

2003

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Metallothioneins (MT) were obtained after purification from metal-exposed clams (Ruditapes decussatus ) using gelpermeation and ion-exchange chromatography. Four cadmium Á/metallothioneins (CdMTs) were resolved by ionexchange chromatography and they all had similar molecular weights, high cadmium content and an absorption spectra indicative of the presence of characteristic Cd Ã/S aggregates. The NH 2 -terminal sequence suggests the presence of at least two class I clam MT isoforms. For the other two putative clam CdMTs isolated, the results of the amino acid determination were inconclusive. One was slightly contaminated and the other one had a blocked NH 2 -terminal. These clam metalothioneins contain glycine, which seems to be a common feature of molluscan MT family and exhibited more similarity to oysters than to mussels. Further investigation on the inducibility of these isoforms will be necessary if clams are to be used as biomarkers of metal exposure. #

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NMR Structure of the Sea Urchin (Strongylocentrotus purpuratus) Metallothionein MTA

Cited by 87 publications

References 49 publications

Structural features specific to plant metallothioneins

Structural features specific to plant metallothioneins

The Metal-Thiolate Clusters of Plant Metallothioneins

Isolation and characterisation of metallothionein from the clam Ruditapes decussatus

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