Template:Sandbox Reserved O'Brochta HLSC322
From Proteopedia
(→HLSC322 Project: Exploring Structure/Function of Genetically Relevant Molecules) |
(→HLSC322 Genetics O'Brochta) |
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| - | == | + | ==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 <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. | ||
Current revision
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.
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