Difference between revisions of "Part:BBa K5205000"
 
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<figcaption><center>Figure 1. Degradation of N-acyl homoserine lactone (AHL) by AiiA. The dashed line on the left shows where the enzyme breaks the bond (Chen et al., 2013; Dong et al., 2000). </center></figcaption>
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<figcaption><center>Figure 1. A. Predicted 3D structure of OsMTI-1b (Jumper et al., 2021; Varadi et al., 2024); B. General structure of metallothionein, with four and three metal ions coordinated in the α- and β-domains, respectively (Klaassen et al., 1999). </center></figcaption>
 
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===Usage and Biology===
 
  
 
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<span class='h3bb'>Sequence and Features</span>
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===Sequence and Features===
 
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===Usage and Biology===
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OsMTI-1b can bind heavy metal ions and act as effective metal removers in water when expressed on the membrane surface.
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===References===
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Buell, C. R., Yuan, Q., Ouyang, S., Liu, J., Zhu, W., Wang, A., Maiti, R., Haas, B., Wortman, J., Pertea, M., Jones, K. M., Kim, M., Overton, L., Tsitrin, T., Fadrosh, D., Bera, J., Weaver, B., Jin, S., Johri, S., . . . Jackson, S. (2005). Sequence, annotation, and analysis of synteny between rice chromosome 3 and diverged grass species. Genome Res, 15(9), 1284-1291. https://doi.org/10.1101/gr.3869505
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Klaassen, C. D., Liu, J., & Choudhuri, S. (1999). Metallothionein: an intracellular protein to protect against cadmium toxicity. Annual review of pharmacology and toxicology, 39, 267-294.
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Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., Bridgland, A., Meyer, C., Kohl, S. A. A., Ballard, A. J., Cowie, A., Romera-Paredes, B., Nikolov, S., Jain, R., Adler, J., Back, T., Petersen, S., Reiman, D., Clancy, E., Zielinski, M., Steinegger, M., Pacholska, M., Berghammer, T., Bodenstein, S., Silver, D., Vinyals, O., Senior, A. W., Kavukcuoglu, K., Kohli, P., & Hassabis, D. (2021). Highly accurate protein structure prediction with AlphaFold. Nature, 596(7873), 583–589. https://doi.org/10.1038/s41586-021-03819-2
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Ruttkay-Nedecky, B., Nejdl, L., Gumulec, J., Zitka, O., Masarik, M., Eckschlager, T., Stiborova, M., Adam, V., & Kizek, R. (2013). The role of metallothionein in oxidative stress. Int J Mol Sci, 14(3), 6044-6066. https://doi.org/10.3390/ijms14036044
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Thirumoorthy, N., Manisenthil Kumar, K. T., Shyam Sundar, A., Panayappan, L., & Chatterjee, M. (2007). Metallothionein: an overview. World J Gastroenterol, 13(7), 993-996. https://doi.org/10.3748/wjg.v13.i7.993
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Varadi, M., Bertoni, D., Magana, P., Paramval, U., Pidruchna, I., Radhakrishnan, M., Tsenkov, M., Nair, S., Mirdita, M., Yeo, J., Kovalevskiy, O., Tunyasuvunakool, K., Laydon, A., Žídek, A., Tomlinson, H., Hariharan, D., Abrahamson, J., Green, T., Jumper, J., Birney, E., Steinegger, M., Hassabis, D., & Velankar, S. (2024). AlphaFold Protein Structure Database in 2024: Providing structure coverage for over 214 million protein sequences. Nucleic Acids Research. https://doi.org/10.1093/nar/gkad117

Latest revision as of 02:44, 24 September 2024


OsMTI-1b, metallothionein from Oryza sativa subsp. japonica

OsMTI-1b (also noted as OsMT1) encodes for a metallothionein (MT) in rice (Oryza sativa subsp. japonica) (Buell et al., 2005). As a metallothionein, OsMTI-1b binds to metal ions, involving metal ion transport, antioxidant defense, and maintaining metal ion balance in rice (Ruttkay-Nedecky et al., 2013; Thirumoorthy et al., 2007). This part is codon-optimized for E. coli.

Figure 1. A. Predicted 3D structure of OsMTI-1b (Jumper et al., 2021; Varadi et al., 2024); B. General structure of metallothionein, with four and three metal ions coordinated in the α- and β-domains, respectively (Klaassen et al., 1999).

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]


Usage and Biology

OsMTI-1b can bind heavy metal ions and act as effective metal removers in water when expressed on the membrane surface.


References

Buell, C. R., Yuan, Q., Ouyang, S., Liu, J., Zhu, W., Wang, A., Maiti, R., Haas, B., Wortman, J., Pertea, M., Jones, K. M., Kim, M., Overton, L., Tsitrin, T., Fadrosh, D., Bera, J., Weaver, B., Jin, S., Johri, S., . . . Jackson, S. (2005). Sequence, annotation, and analysis of synteny between rice chromosome 3 and diverged grass species. Genome Res, 15(9), 1284-1291. https://doi.org/10.1101/gr.3869505

Klaassen, C. D., Liu, J., & Choudhuri, S. (1999). Metallothionein: an intracellular protein to protect against cadmium toxicity. Annual review of pharmacology and toxicology, 39, 267-294.

Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., Bridgland, A., Meyer, C., Kohl, S. A. A., Ballard, A. J., Cowie, A., Romera-Paredes, B., Nikolov, S., Jain, R., Adler, J., Back, T., Petersen, S., Reiman, D., Clancy, E., Zielinski, M., Steinegger, M., Pacholska, M., Berghammer, T., Bodenstein, S., Silver, D., Vinyals, O., Senior, A. W., Kavukcuoglu, K., Kohli, P., & Hassabis, D. (2021). Highly accurate protein structure prediction with AlphaFold. Nature, 596(7873), 583–589. https://doi.org/10.1038/s41586-021-03819-2

Ruttkay-Nedecky, B., Nejdl, L., Gumulec, J., Zitka, O., Masarik, M., Eckschlager, T., Stiborova, M., Adam, V., & Kizek, R. (2013). The role of metallothionein in oxidative stress. Int J Mol Sci, 14(3), 6044-6066. https://doi.org/10.3390/ijms14036044

Thirumoorthy, N., Manisenthil Kumar, K. T., Shyam Sundar, A., Panayappan, L., & Chatterjee, M. (2007). Metallothionein: an overview. World J Gastroenterol, 13(7), 993-996. https://doi.org/10.3748/wjg.v13.i7.993

Varadi, M., Bertoni, D., Magana, P., Paramval, U., Pidruchna, I., Radhakrishnan, M., Tsenkov, M., Nair, S., Mirdita, M., Yeo, J., Kovalevskiy, O., Tunyasuvunakool, K., Laydon, A., Žídek, A., Tomlinson, H., Hariharan, D., Abrahamson, J., Green, T., Jumper, J., Birney, E., Steinegger, M., Hassabis, D., & Velankar, S. (2024). AlphaFold Protein Structure Database in 2024: Providing structure coverage for over 214 million protein sequences. Nucleic Acids Research. https://doi.org/10.1093/nar/gkad117