NDLI: The metal-binding properties of the blue crab copper specific CuMT-2: a crustacean metallothionein with two cysteine triplets.

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The metal-binding properties of the blue crab copper specific CuMT-2: a crustacean metallothionein with two cysteine triplets.

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The metal-binding properties of the blue crab copper specific CuMT-2: a crustacean metallothionein with two cysteine triplets.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Serra-Batiste, Montserrat Cols, Neus Alcaraz, Luis A. Donaire, Antonio González-Duarte, Pilar Vasák, Milan
Description	Country affiliation: Spain Author Affiliation: Serra-Batiste M ( Departament de Química, Universitat Autònoma de Barcelona, Bellaterra, Spain.)
Abstract	Most crustacean metallothioneins (MTs) contain 18 Cys residues and bind six divalent metal ions. The copper-specific CuMT-2 (MTC) of the blue crab Callinectes sapidus with 21 Cys residues, of which six are organized in two uncommon Cys-Cys-Cys sequences, represents an exception. However, its metal-binding properties are unknown. By spectroscopic and spectrometric techniques we show that all 21 Cys residues of recombinant MTC participate in the binding of Cu(I), Zn(II), and Cd(II) ions, indicating that both Cys triplets act as ligands. The fully metallated M(8) (II)-MTC (M is Zn, Cd) form possesses high- and low-affinity metal binding sites, as evidenced by the formation of Zn(6)-MTC and Cd(7)-MTC species from M(8) (II)-MTC after treatment with Chelex 100. The NMR characterization of Cd(7)-MTC suggests the presence of a two-domain structure, each domain containing one Cys triplet and encompassing either the three-metal or the four-metal thiolate cluster. Whereas the metal-Cys connectivities in the three-metal cluster located in the N-terminal domain (residues 1-31) reveal a Cd(3)Cys(9) cyclohexane-like structure, the presence of dynamic processes in the C-terminal domain (residues 32-64) precluded the determination of the organization of the four-metal cluster. Absorption and circular dichroism features accompanying the stepwise binding of Cu(I) to MTC suggest that all 21 Cys are involved in the binding of eight to nine Cu(I) ions (Cu(8-9)-MTC). The subsequent generation of Cu(12)-MTC involves structural changes consistent with a decrease in the Cu(I) coordination number. Overall, the metal-binding properties of MTC reported here contribute to a better understanding of the role of Cys triplets in MTs.
File Format	HTM / HTML
ISSN	09498257
Issue Number	5
Volume Number	15
e-ISSN	14321327
Journal	JBIC Journal of Biological Inorganic Chemistry
Language	English
Publisher	Springer
Publisher Date	2010-06-01
Publisher Place	Germany
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Discipline Biochemistry Brachyura Chemistry Copper Metabolism Cysteine Metallothionein Metals Animals Binding Sites Cadmium Ligands Isolation & Purification Recombinant Proteins Zinc Journal Article Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Biochemistry Inorganic Chemistry

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