From Proteopedia
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'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.
| Heterodimer </scene> 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.
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Structure of E. coli Transcription Initiation Complex
| This is a 27 chain protein structure with 11244 amino acid alpha carbons. Like DNA polymerase, this complex is made up of multiple polypeptide chains with four different types of subunits, called alpha, beta, beta prime, and omega. RNA polymerase forms a holoenzyme when the sigma factor binds to the omega sub unit. The sigma factor is relatively weak and can be separated leaving a core polymerase. The core polymerase can catalyze the polymerization of DNA into RNA by its self. The sigma factor is not required for the basic catalytic activity of the enzyme however, the core polymerase cannot bind to the proper DNA sequence without it.
Function
This sigma factor allows the RNA polymerase to bind to the -35 and -10 consensus sequences so that the RNA polymerase active site is aligned with the start site. Once the RNA polymerase undergoes morphological changes, the RNA polymerase begins abortive transcription and the sigma factor can leave the complex. After this has been completed, transcription begins.
Location
In prokaryotic cells transcription and translation are coupled. The catalytic activity of the complex takes place in the cytoplasm of the prokaryote E. coli. E. coli is a gram-negative bacterium that is commonly found in the lower intestine of warm-blooded organisms.
Interactions between the DNA, RNA Polymerase, and Sigma Factor
The (highlighted in magenta) binds to the RNA polymerase at the (highlighted in black) in the same orientation as the beta subunit. As mentioned previously, the sigma factor binds to the consensus sequences on the target (highlighted in orange) in order to set the RNA polymerase above the start site.
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