Sandbox Reserved 1263

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== Structure ==
== Structure ==
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The <scene name='75/751156/Overall_molecule/1'>overall DNA molecule</scene> is a double-helix.
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The <scene name='75/751156/Overall_dna_molecule/1''>overall DNA molecule</scene> is a double-helix.
== Function ==
== Function ==
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== Structural highlights ==
== Structural highlights ==
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This is a sample scene created with SAT to <scene name="/75/751156/Overall_molecule/1">green</scene> by Jessica Yin.
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This is a sample scene created with SAT to <scene name="/75/751156/Overall_dna_molecule/1'">green</scene> by Jessica Yin.
</StructureSection>
</StructureSection>
== References ==
== References ==
<references/>
<references/>

Revision as of 21:18, 31 January 2017

Contents

genetics is ok

'Molecules it Interacts With and where '

The protein binds to GDP as well as the following ligands in order to promote the attachment of the protein complex to the ribosome A site.

PHOSHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER


PHENYLALANINE MAGNESIUM ION


'Origin'

It has domains that are created in yeast (phenyl-transfer RNA) , in the heat resistant Thermus aquaticus (EF-Tu elongation factor, and can be synthetically manufactured.


'Structure'

It has 3 domains. G proteins, Elongation Factors, and the EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain. It is composed of 6 chains, which combine in alignment.


Specific are highlighted here. The ligands listed above, GDP, Phe, and Mg+2 ion each attach at these locations which are still being explored.

which play a crucial role in binding to the ribosome during translation. They form positive pockets with which negative amino acids can bind to.

'Molecules it Interacts With and where '

The protein binds to GDP as well as the following ligands in order to promote the attachment of the protein complex to the ribosome A site.

PHOSHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER


PHENYLALANINE MAGNESIUM ION


'Origin'

It has domains that are created in yeast (phenyl-transfer RNA) , in the heat resistant Thermus aquaticus (EF-Tu elongation factor, and can be synthetically manufactured.


'Structure'

It has 3 domains. G proteins, Elongation Factors, and the EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain. It is composed of 6 chains, which combine in alignment.


Specific are highlighted here.

which play a crucial role in binding to the ribosome during translation.

'Function"

The protein complex participates in placing the amino acids in their correct order when messenger RNA is translated into a protein sequence on the ribosome by promoting GTP-dependent binding of tRNA to the A site of the ribosome. In other words, it is involved with elongation during polypeptide synthesis.

Phe-tRNA, elongation factor EF-TU:GDPNP Ternary complex

Drag the structure with the mouse to rotate

Deoxyribonucleic acid (DNA)

PDB ID 1bna

Drag the structure with the mouse to rotate

References

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