Template:Sandbox Reserved O'Brochta HLSC322

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==HLSC322 Project: Exploring Structure/Function of Genetically Relevant Molecules==
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==genetics is ok==
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'''Objective:''' You will investigate the structure and function of a genetically relevant molecule (you have been assigned a molecule).
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You will use this page to create a short report that highlights the relevant structural features that relate to the molecules function.
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''We are exploring structure to help us appreciate the chemical basis of heredity and to begin to understand how structures of proteins is tied to their functions''
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=='Molecules it Interacts With and where '==
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'''YOU ARE STRONGLY ENCOURAGED TO WORK WITH WITH OTHER TEAMS TO COMPLETE THIS PROJECT!'''
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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.
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For help along the way you should consult [[Proteopedia:Video Guide]] or [[Help:Getting Started in Proteopedia]] <br>
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''PHOSHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER''
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For more help on marking up a Wiki page you can check this Cheatsheet[https://en.wikipedia.org/wiki/Help:Cheatsheet]<br><br>
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==
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Instructions: ==
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1. ALWAYS 'SAVE PAGE' FREQUENTLY WHILE YOU ARE WORKING. (this is a Wiki and all versions will be available)<br>
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''PHENYLALANINE''
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2. '''Introduction:''' This should be a brief (≤250 words), clear exposition that orients the reader to the genetic process involved and the role of your molecule in this process.<br>
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''MAGNESIUM ION''
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3. Load an applet of your molecule (place it and size it to your liking)<br>
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4. '''About {your molecule's name}'''<br>
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=='Origin'==
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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.
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=='Structure'==
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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.
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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.
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<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.
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=='Molecules it Interacts With and where '==
 +
 
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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.
 +
 
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''PHOSHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER''
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''PHENYLALANINE''
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''MAGNESIUM ION''
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=='Origin'==
 +
 
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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'==
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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"==
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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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<Structure load='1ttt' size='350' frame='true' align='right' caption='Phe-tRNA, elongation factor EF-TU:GDPNP Ternary complex'
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=='Molecules it Interacts With and where '==
 +
 
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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.

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

Drag the structure with the mouse to rotate
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