Sandbox Reserved 1508
From Proteopedia
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<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> | <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> | ||
The protein 5C04 is classified as an oxidoreductase. We found it in the ''Mycobacterium tuberculosis'' organism, especially in the strain ATCC 25618/H37Rv. It can be expressed in ''Escherichia Coli'' bacteria. This is a pathogenic protein which is involved in the tuberculosis. Its pathogenicity is due to a specific mutation in the active site of peroxiredoxins. | The protein 5C04 is classified as an oxidoreductase. We found it in the ''Mycobacterium tuberculosis'' organism, especially in the strain ATCC 25618/H37Rv. It can be expressed in ''Escherichia Coli'' bacteria. This is a pathogenic protein which is involved in the tuberculosis. Its pathogenicity is due to a specific mutation in the active site of peroxiredoxins. | ||
- | <ref>DOI: 10.2210/pdb5C04/pdb | + | <ref>DOI: 10.2210/pdb5C04/pdb/<ref> |
Revision as of 17:42, 10 January 2019
This Sandbox is Reserved from 06/12/2018, through 30/06/2019 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1480 through Sandbox Reserved 1543. |
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The protein 5C04
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References
Ågren, Daniel, Robert Schnell, Wulf Oehlmann, Mahavir Singh, et Gunter Schneider. « Cysteine Synthase (CysM) of Mycobacterium Tuberculosis Is an O -Phosphoserine Sulfhydrylase: EVIDENCE FOR AN ALTERNATIVE CYSTEINE BIOSYNTHESIS PATHWAY IN MYCOBACTERIA ». Journal of Biological Chemistry 283, nᵒ 46 (14 novembre 2008): 31567‑74. https://doi.org/10.1074/jbc.M804877200.
Burns, Kristin E., Sabine Baumgart, Pieter C. Dorrestein, Huili Zhai, Fred W. McLafferty, et Tadhg P. Begley. « Reconstitution of a New Cysteine Biosynthetic Pathway in Mycobacterium t Uberculosis ». Journal of the American Chemical Society 127, nᵒ 33 (août 2005): 11602‑3. https://doi.org/10.1021/ja053476x.
Pedre, Brandán, Laura A. H. van Bergen, Anna Palló, Leonardo A. Rosado, Veronica Tamu Dufe, Inge Van Molle, Khadija Wahni, et al. « The Active Site Architecture in Peroxiredoxins: A Case Study on Mycobacterium Tuberculosis AhpE ». Chemical Communications 52, nᵒ 67 (2016): 10293‑96. https://doi.org/10.1039/C6CC02645A.
Rhee, Sue Goo, et Hyun Ae Woo. « Multiple Functions of Peroxiredoxins: Peroxidases, Sensors and Regulators of the Intracellular Messenger H 2 O 2 , and Protein Chaperones ». Antioxidants & Redox Signaling 15, nᵒ 3 (août 2011): 781‑94. https://doi.org/10.1089/ars.2010.3393.
Zeida, Ari, Aníbal M. Reyes, Pablo Lichtig, Martín Hugo, Diego S. Vazquez, Javier Santos, F. Luis González Flecha, Rafael Radi, Dario A. Estrin, et Madia Trujillo. « Molecular Basis of Hydroperoxide Specificity in Peroxiredoxins: The Case of AhpE from Mycobacterium Tuberculosis ». Biochemistry 54, nᵒ 49 (15 décembre 2015): 7237‑47. https://doi.org/10.1021/acs.biochem.5b00758.