Sandbox Reserved 1263
From Proteopedia
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==Structure== | ==Structure== | ||
<StructureSection load='1bna' size='340' side='r> | <StructureSection load='1bna' size='340' side='r> | ||
- | The <scene name='75/751156/Overall_molecule/1'>overall DNA molecule</scene> is a double-helix. | ||
== Headline text == | == Headline text == | ||
- | ight' caption=' | + | ight' caption='DNA Molecule' scene=''> |
- | + | The <scene name='75/751156/Overall_molecule/1'>overall DNA molecule</scene> is a double-helix. | |
- | + | ||
== Function == | == Function == | ||
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- | == Disease == | ||
== Relevance == | == Relevance == | ||
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== Structural highlights == | == Structural highlights == | ||
- | This is a sample scene created with SAT to <scene name="/ | + | This is a sample scene created with SAT to <scene name="/75/751156/Overall_molecule/1">green</scene> by Jessica Yin. |
- | + | ||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> |
Revision as of 21:11, 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.
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Structure
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