Sandbox Reserved 962

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<scene name='60/604481/Interaction_gtg/1'>6 amino acids</scene> are involded in the binding of the cap analog.
<scene name='60/604481/Interaction_gtg/1'>6 amino acids</scene> are involded in the binding of the cap analog.
The cap makes Van der Walls contacts, hydrogen bond and water mediated bond.
The cap makes Van der Walls contacts, hydrogen bond and water mediated bond.
 +
=== AdoHcy Binding (S-adenosyl-L-homocysteine)===
=== AdoHcy Binding (S-adenosyl-L-homocysteine)===
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<scene name='60/604481/Interaction_sah/1'>10 amino acids</scene> (Lys54, Gly72, Asp78, Asp94, Ile95, Asp122, Ser124, Gln140, Phe141, Ser142) are involved in the stabilisation of AdoHcys.
<scene name='60/604481/Interaction_sah/1'>10 amino acids</scene> (Lys54, Gly72, Asp78, Asp94, Ile95, Asp122, Ser124, Gln140, Phe141, Ser142) are involved in the stabilisation of AdoHcys.
The interactions between AdoHcys and the enzyme are made of : hydrogen bonds, Van der Walls interactions,electrostatic interaction and water mediated contact.
The interactions between AdoHcys and the enzyme are made of : hydrogen bonds, Van der Walls interactions,electrostatic interaction and water mediated contact.
 +
<ref>Fabrega C, Hausmann S, Shen V, Shuman S, Lima CD. Structure and mechanism of mRNA cap (guanine-N7) methyltransferase. Mol Cell. 2004 Jan 16;13(1):77-89. PMID:14731396</ref>
== Post transcriptional modifications==
== Post transcriptional modifications==
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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
 
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</StructureSection>
 
== References ==
== References ==
<references/>
<references/>

Revision as of 15:25, 29 December 2014

This Sandbox is Reserved from 15/11/2014, through 15/05/2015 for use in the course "Biomolecule" taught by Bruno Kieffer at the Strasbourg University. This reservation includes Sandbox Reserved 951 through Sandbox Reserved 975.
To get started:
  • Click the edit this page tab at the top. Save the page after each step, then edit it again.
  • Click the 3D button (when editing, above the wikitext box) to insert Jmol.
  • show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page.
  • Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc.

More help: Help:Editing


mRNA Cap (Guanine-N7) Methyltransferase (Ecm1)


Ecm1

Drag the structure with the mouse to rotate


Contents

Function

Structure

Interaction

Cap Analog Binding (7-methylguanosine-5-triphosphate-5-Guanosine)

binds to the enzyme in a pocket near the AdoHcy. are involded in the binding of the cap analog. The cap makes Van der Walls contacts, hydrogen bond and water mediated bond.


AdoHcy Binding (S-adenosyl-L-homocysteine)

The mRNA Cap Methyltransferase bind to which is the product of the methyl donor AdoMet after the methylation. AdoHcys is in a pocket formed by amino acids of segment 2. (Lys54, Gly72, Asp78, Asp94, Ile95, Asp122, Ser124, Gln140, Phe141, Ser142) are involved in the stabilisation of AdoHcys. The interactions between AdoHcys and the enzyme are made of : hydrogen bonds, Van der Walls interactions,electrostatic interaction and water mediated contact. [1]

Post transcriptional modifications

References

  1. ↑ Fabrega C, Hausmann S, Shen V, Shuman S, Lima CD. Structure and mechanism of mRNA cap (guanine-N7) methyltransferase. Mol Cell. 2004 Jan 16;13(1):77-89. PMID:14731396
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