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{{Sandbox_Reserved_O'Brochta_HLSC322}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->
 
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==Your Heading Here (maybe something like 'Structure')==
 
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<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
 
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This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
 
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You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
 
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== References ==
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=='Function"==
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H.M. Berman, J. Westbrook, Z. Feng, G. Gilliland, T.N. Bhat, H. Weissig, I.N. Shindyalov, P.E. Bourne.
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(2000) The Protein Data Bank Nucleic Acids Research, 28: 235-242.
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== Disease ==
 
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== Relevance ==
 
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== Structural highlights ==
 
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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>
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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.
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== References ==
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<references/>
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<Structure load='1ttt' size='350' frame='true' align='right' caption='Phe-tRNA, elongation factor EF-TU:GDPNP Ternary complex'
 +
 
 +
=='Function"==
 +
 
 +
 
 +
 
 +
 
 +
 
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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.
 +
 
 +
<Structure load='1ttt' size='350' frame='true' align='right' caption='Phe-tRNA, elongation factor EF-TU:GDPNP Ternary complex'
 +
 
 +
=='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 <scene name='75/751161/Hetero_domains/1'>Heterodimer </scene> alignment.
 +
 
 +
 
 +
Specific <scene name='75/751161/Ligand_site/1'>Ligand Sites</scene> are highlighted here. The ligands listed above, GDP, Phe, and Mg+2 ion each attach at these locations which are still being explored.
 +
 
 +
<scene name='75/751161/Basic_positive_residues/2'>Basic and Positive Residues</scene> 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 <scene name='75/751161/Hetero_domains/1'>Heterodimer </scene> alignment.
 +
 
 +
 
 +
Specific <scene name='75/751161/Ligand_site/1'>Ligand Sites</scene> are highlighted here.
 +
 
 +
<scene name='75/751161/Basic_positive_residues/2'>Basic and Positive Residues</scene> which play a crucial role in binding to the ribosome during translation.
 +
 
 +
=='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 <scene name='75/751161/Hetero_domains/1'>Heterodimer </scene> alignment.
 +
 
 +
 
 +
Specific <scene name='75/751161/Ligand_site/1'>Ligand Sites</scene> are highlighted here. The ligands listed above, GDP, Phe, and Mg+2 ion each attach at these locations which are still being explored.
 +
 
 +
<scene name='75/751161/Basic_positive_residues/2'>Basic and Positive Residues</scene> 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 <scene name='75/751161/Hetero_domains/1'>Heterodimer </scene> alignment.
 +
 
 +
 
 +
Specific <scene name='75/751161/Ligand_site/1'>Ligand Sites</scene> are highlighted here.
 +
 
 +
<scene name='75/751161/Basic_positive_residues/2'>Basic and Positive Residues</scene> 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.
 +
 
 +
<Structure load='1ttt' size='350' frame='true' align='right' caption='Phe-tRNA, elongation factor EF-TU:GDPNP Ternary complex'
 +
 
 +
=='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 <scene name='75/751161/Hetero_domains/1'>Heterodimer </scene> alignment.
 +
 
 +
 
 +
Specific <scene name='75/751161/Ligand_site/1'>Ligand Sites</scene> are highlighted here. The ligands listed above, GDP, Phe, and Mg+2 ion each attach at these locations which are still being explored.
 +
 
 +
<scene name='75/751161/Basic_positive_residues/2'>Basic and Positive Residues</scene> 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 <scene name='75/751161/Hetero_domains/1'>Heterodimer </scene> alignment.
 +
 
 +
 
 +
Specific <scene name='75/751161/Ligand_site/1'>Ligand Sites</scene> are highlighted here.
 +
 
 +
<scene name='75/751161/Basic_positive_residues/2'>Basic and Positive Residues</scene> which play a crucial role in binding to the ribosome during translation.
 +
 
 +
=='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 <scene name='75/751161/Hetero_domains/1'>Heterodimer </scene> alignment.
 +
 
 +
 
 +
Specific <scene name='75/751161/Ligand_site/1'>Ligand Sites</scene> are highlighted here. The ligands listed above, GDP, Phe, and Mg+2 ion each attach at these locations which are still being explored.
 +
 
 +
<scene name='75/751161/Basic_positive_residues/2'>Basic and Positive Residues</scene> 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 <scene name='75/751161/Hetero_domains/1'>Heterodimer </scene> alignment.
 +
 
 +
 
 +
Specific <scene name='75/751161/Ligand_site/1'>Ligand Sites</scene> are highlighted here.
 +
 
 +
<scene name='75/751161/Basic_positive_residues/2'>Basic and Positive Residues</scene> which play a crucial role in binding to the ribosome during translation.

Current revision

'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

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