Related ArticlesStructural Adaptation of a Protein to Increased Metal Stress: NMR Structure of a Marine Snail Metallothionein with an Additional Domain.
Angew Chem Int Ed Engl. 2017 Mar 23;:
Authors: Baumann C, Beil A, Jurt S, Niederwanger M, Palacios O, Capdevila M, Atrian S, Dallinger R, Zerbe O
Abstract
In this study, we present an NMR structure of the metallothionein (MT) from the snail Littorina littorea (LlMT) in complex with Cd(2+) . LlMT is capable of binding 9 Zn(2+) or 9 Cd(2+) 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 ?2 and C-terminal ? 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 ?1 and ?2 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(2+) stress and adverse environmental conditions.
PMID: 28332759 [PubMed - as supplied by publisher]
Heavy metal binding domain in a cysteine-rich protein may be sea snail adaptation to metal stress - Phys.Org
Heavy metal binding domain in a cysteine-rich protein may be sea snail adaptation to metal stress - Phys.Org
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Heavy metal binding domain in a cysteine-rich protein may be sea snail adaptation to metal stress
Phys.Org
Structural Adaptation of a Protein to Increased Metal Stress: NMR Structure of a Marine Snail Metallothionein with an Additional Domain. Credit: Wiley. A special type of small sulfur-rich protein, metallothioneins, have an extraordinary capability for ...
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Maximum occurrence analysis of protein conformations for different distributions of paramagnetic metal ions within flexible two-domain proteins
Maximum occurrence analysis of protein conformations for different distributions of paramagnetic metal ions within flexible two-domain proteins
Publication year: 2012
Source:Journal of Magnetic Resonance, Volume 215</br>
Claudio Luchinat, Malini Nagulapalli, Giacomo Parigi, Luca Sgheri</br>
Multidomain proteins are composed of rigid domains connected by (flexible) linkers. Therefore, the domains may experience a large degree of reciprocal reorientation. Pseudocontact shifts and residual dipolar couplings arising from one or more paramagnetic metals successively placed...
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03-09-2012 09:16 AM
Maximum occurrence analysis of protein conformations for different distributions of paramagnetic metal ions within flexible two-domain proteins
Maximum occurrence analysis of protein conformations for different distributions of paramagnetic metal ions within flexible two-domain proteins
Publication year: 2011
Source: Journal of Magnetic Resonance, Available online 30 December 2011</br>
Claudio*Luchinat, Malini*Nagulapalli, Giacomo*Parigi, Luca*Sgheri</br>
Multidomain proteins are composed of rigid domains connected by (flexible) linkers. Therefore, the domains may experience a large degree of reciprocal reorientation. Pseudocontact shifts and residual dipolar couplings arising from one or more paramagnetic metals successively...
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12-31-2011 10:40 AM
[NMR paper] Solution NMR structure of ribosome-binding factor A (RbfA), a cold-shock adaptation p
Solution NMR structure of ribosome-binding factor A (RbfA), a cold-shock adaptation protein from Escherichia coli.
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J Mol Biol. 2003 Mar 21;327(2):521-36
Authors: Huang YJ, Swapna GV, Rajan PK, Ke H, Xia B, Shukla K, Inouye M, Montelione GT
Ribosome-binding factor A (RbfA) from Escherichia coli is a cold-shock adaptation protein. It is essential for efficient processing of 16S rRNA and is suspected to interact with...
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11-24-2010 09:01 PM
[NMR paper] 111Cd NMR studies of the domain specificity of Ag+ and Cu+ binding to metallothionein
111Cd NMR studies of the domain specificity of Ag+ and Cu+ binding to metallothionein.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles 111Cd NMR studies of the domain specificity of Ag+ and Cu+ binding to metallothionein.
Biochemistry. 1996 Nov 5;35(44):13929-36
Authors: Li H, Otvos JD
Metal displacement reactions of Cd7MT with Ag+ or Cu+ and interprotein metal exchange reactions between Cd7MT and Ag12MT or Cu12MT were studied by 111Cd NMR. Titration of 111Cd7MT with Ag+ indicates that...
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08-22-2010 02:20 PM
[NMR paper] Mutation of invariant cysteines of mammalian metallothionein alters metal binding cap
Mutation of invariant cysteines of mammalian metallothionein alters metal binding capacity, cadmium resistance, and 113Cd NMR spectrum.
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J Biol Chem. 1991 Dec 25;266(36):24390-7
Authors: Cismowski MJ, Narula SS, Armitage IM, Chernaik ML, Huang PC
Using a yeast expression vector system, we have expressed both wild type and six mutated Chinese hamster metallothionein coding sequences in a...
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08-21-2010 11:12 PM
[NMR paper] Mutation of invariant cysteines of mammalian metallothionein alters metal binding cap
Mutation of invariant cysteines of mammalian metallothionein alters metal binding capacity, cadmium resistance, and 113Cd NMR spectrum.
Related Articles Mutation of invariant cysteines of mammalian metallothionein alters metal binding capacity, cadmium resistance, and 113Cd NMR spectrum.
J Biol Chem. 1991 Dec 25;266(36):24390-7
Authors: Cismowski MJ, Narula SS, Armitage IM, Chernaik ML, Huang PC
Using a yeast expression vector system, we have expressed both wild type and six mutated Chinese hamster metallothionein coding sequences in a...
Structural Adaptation of a Protein to Increased Metal Stress: NMR Structure of a Marine Snail Metallothionein with an Additional Domain.
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