Difference between revisions of "Part:BBa K3275001"
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=Introduction=
 
=Introduction=
 
==Background==
 
==Background==
−
Metallothionein (MT) is a class of small metal-binding proteins that exists in bacteria, plants and animals. These proteins depending on their amino acid compositions have a high binding affinity with different bivalent metal ions. Once MT detects the corresponding metal, it binds the goal through covalent bonds, which are composed of sulfhydryl cysteine residues and stores the metal by tightly chelating the metal. Typically, it is assumed that MTs have two binding domains, one of which is the C-terminal part (α-domain) with three binding sites. The other one is the N-terminal part (β-domain) with four divalent binding sites <ref>Vasak, M. and Kagi, J. (1981). Metal thiolate clusters in cobalt(II)-metallothionein. Proceedings of the National Academy of Sciences, 78(11), pp.6709-6713.</ref>. Therefore, MTs are important for protecting the cell against heavy metal toxicity and maintaining cellular homeostasis.
+
Metallothionein (MT) is a class of small metal-binding proteins that exists in bacteria, plants and animals. These proteins depending on their amino acid compositions have a high binding affinity with different bivalent metal ions. Once MT detects the corresponding metal, it binds the goal through covalent bonds, which are composed of sulfhydryl cysteine residues and stores the metal by tightly chelating the metal. Typically, it is assumed that MTs have two binding domains, one of which is the C-terminal part (α-domain) with three binding sites. The other one is the N-terminal part (β-domain) with four divalent binding sites <ref> Ruttkay-Nedecky, B., Nejdl, L., Gumulec, J., Zitka, O., Masarik, M., Eckschlager, T., … Kizek, R. (2013). The role of metallothionein in oxidative stress. International journal of molecular sciences, 14(3), 6044–6066. doi:10.3390/ijms14036044</ref>. Therefore, MTs are important for protecting the cell against heavy metal toxicity and maintaining cellular homeostasis.
 
==Cobalt Metallothionein==
 
==Cobalt Metallothionein==
 
=Characterization=
 
=Characterization=
 
=References=
 
=References=
−
Vasak, M. and Kagi, J. (1981). Metal thiolate clusters in cobalt(II)-metallothionein. Proceedings of the National Academy of Sciences, 78(11), pp.6709-6713.
 

Revision as of 19:22, 8 October 2019


Cobalt Metallothionein

Oryctolagus cuniculus cobalt targeting metallothionein.

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal BamHI site found at 3
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]



Introduction

Background

Metallothionein (MT) is a class of small metal-binding proteins that exists in bacteria, plants and animals. These proteins depending on their amino acid compositions have a high binding affinity with different bivalent metal ions. Once MT detects the corresponding metal, it binds the goal through covalent bonds, which are composed of sulfhydryl cysteine residues and stores the metal by tightly chelating the metal. Typically, it is assumed that MTs have two binding domains, one of which is the C-terminal part (α-domain) with three binding sites. The other one is the N-terminal part (β-domain) with four divalent binding sites [1]. Therefore, MTs are important for protecting the cell against heavy metal toxicity and maintaining cellular homeostasis.

Cobalt Metallothionein

Characterization

References

  1. ↑ Ruttkay-Nedecky, B., Nejdl, L., Gumulec, J., Zitka, O., Masarik, M., Eckschlager, T., … Kizek, R. (2013). The role of metallothionein in oxidative stress. International journal of molecular sciences, 14(3), 6044–6066. doi:10.3390/ijms14036044