Sandbox Reserved 1481
From Proteopedia
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== Cristal structure == | == Cristal structure == | ||
- | To study the crital structure of the METTL3/METTL14 some cristalograghy experiments have been realizes under the following experimental conditions : | + | To study the crital structure of the METTL3/METTL14 some cristalograghy experiments have been realizes under the following experimental conditions to cristalyze the protein complex: |
'''Method''' : Vapor Diffusion Hanging Drop | '''Method''' : Vapor Diffusion Hanging Drop | ||
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'''Buffer''': 0.1 M Tris pH 8.0, 20% PEG3350 | '''Buffer''': 0.1 M Tris pH 8.0, 20% PEG3350 | ||
+ | After critalization, cristal had been analyzed through X-Ray diffraction, at 100°C, with a single wavelength coming out of a synchrotron. | ||
Thanks to the experiment the following data have been collected to describe the cristal structure of the complex : | Thanks to the experiment the following data have been collected to describe the cristal structure of the complex : | ||
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Space Group''' P 41 21 2 | Space Group''' P 41 21 2 | ||
- | The primitive cubic symmetry of the unit cell is driven by | + | The primitive cubic symmetry of the unit cell is driven by two 2-fold axis rotation. Moreover, within this space group which is acentric, chiral, and enantiomorphic with one single lattice translations, eight different representative symmetry operations are needed to get the whole unit cell. |
[[Image:Cristallo.jpeg]] | [[Image:Cristallo.jpeg]] | ||
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+ | |||
== Modification processes == | == Modification processes == |
Revision as of 12:39, 27 December 2018
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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Crystal structure of the catalytic domains of Mettl3/Mettl14 complexInsert caption here
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The complex METTL3/METTL14 is a heterodimer enzymatic complex involved into RNA post-transcription modifications by humans. This complex is abble to add a methyl group on adenosin of the RNA, by catalyzing a m6(A) modification.The N(6)-methyladenosine (m(6)A) is a quite common, reversible chemical modifications of RNAs molecules which plays a key role in several biological fonctions. This post transcriptional modification can be added by WRITERS, recognized by READERS and also removed byr ERASERS. The METTL3/METTL14 complex plays the role of writer.
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References
<Structural Basis for Cooperative Function of Mettl3 and Mettl14 Methyltransferases/>[1] <Structural basis of N(6)-adenosine methylation by the METTL3-METTL14 complex./>[2]
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644