Sandbox Reserved 1481

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Thanks to their primary amino acid sequences both A and B chains have some specific conserved domains directly linked to their function and functionning.
Thanks to their primary amino acid sequences both A and B chains have some specific conserved domains directly linked to their function and functionning.
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== Cristal structure ==
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To study the crital structure of the METTL3/METTL14 some cristalograghy experiments have been realizes under the following experimental conditions :
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Method : Vapor Diffusion Hanging Drop
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pH 8
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Temperature : 291.0 K
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Buffer: 0.1 M Tris pH 8.0, 20% PEG3350
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Thanks to the experiment the following data have been collected to describe the cristal structure of the complex :
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Unit Cell caracteristics :
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Length (Å) Angle (°)
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a = 101.86 α = 90
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b = 101.86 β = 90
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c = 117.66 γ = 90
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Symmetry :
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Space Group P 41 21 2
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The primitive cubic symmetry of the unit cell is driven by X Z 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.
== Modification processes ==
== Modification processes ==

Revision as of 10:38, 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 complex

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The complex METTL3/METTL14 is a heterodimer enzymatic complex involved into RNA post-transcription modifications. 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.

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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]

  1. 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
  2. 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
[3]

[4]


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