Difference between revisions of "Part:BBa K3275001"

(→‎Cobalt Metallothionein)
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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.
 
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==
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[[part:BBa K3275001]] is originally from Rainbow trout metallothionein, which is called MTA (Metallothionein A) that has similar structures with Metallothionein-1A. [https://parts.igem.org/Part:BBa_K3275000 Learn more from here.] Both MTs have α and β domains that contain 11 and 9 cysteines. Figure 1 shows the structure of MTA <ref>SWISS-MODEL Repository | P68503. (2019). Retrieved from https://swissmodel.expasy.org/repository/uniprot/P68503?csm=901A8E8084A63EFA</ref>.  
+
[[part:BBa K3275001]] is originally from Rainbow trout metallothionein, which is called MTA (Metallothionein A) that has similar structures with Metallothionein-1A ([[part:BBa_K3275000]]). Both MTs have α and β domains that contain 11 and 9 cysteines. Figure 1 shows the structure of MTA <ref>SWISS-MODEL Repository | P68503. (2019). Retrieved from https://swissmodel.expasy.org/repository/uniprot/P68503?csm=901A8E8084A63EFA</ref>.  
 
[[Image:T--RHIT--RHIT MTA.png|center|frame|300px|<b>Figure 1. </b> 3-D structure of MTA [https://swissmodel.expasy.org/repository/uniprot/P68503?csm=901A8E8084A63EFA find more here]]]
 
[[Image:T--RHIT--RHIT MTA.png|center|frame|300px|<b>Figure 1. </b> 3-D structure of MTA [https://swissmodel.expasy.org/repository/uniprot/P68503?csm=901A8E8084A63EFA find more here]]]
−
For [[part:BBa_K3275000]], some bases from the original sequence are changed due to synthesis demands.
+
For [[part:BBa_K3275001]], some bases from the original sequence are changed due to synthesis demands.
  
 
=Characterization=
 
=Characterization=
 
=References=
 
=References=

Revision as of 16:23, 9 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

part:BBa K3275001 is originally from Rainbow trout metallothionein, which is called MTA (Metallothionein A) that has similar structures with Metallothionein-1A (part:BBa_K3275000). Both MTs have α and β domains that contain 11 and 9 cysteines. Figure 1 shows the structure of MTA [2].

Figure 1. 3-D structure of MTA find more here

For part:BBa_K3275001, some bases from the original sequence are changed due to synthesis demands.

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
  2. ↑ SWISS-MODEL Repository | P68503. (2019). Retrieved from https://swissmodel.expasy.org/repository/uniprot/P68503?csm=901A8E8084A63EFA