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From Proteopedia
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==Connor McDermott and Niall Cope's Structure:E.coli RNA Polymerase sigma-70 Holoenzyme== | ==Connor McDermott and Niall Cope's Structure:E.coli RNA Polymerase sigma-70 Holoenzyme== | ||
| - | <Structure load='4yg2' size='350' frame='true' align=' | + | <Structure load='4yg2' size='350' frame='true' align='center' caption='RNA Polymerase' scene='Insert optional scene name here' /> |
== Functions == | == Functions == | ||
First, regular RNA polymerase II binds to the sigma factor, sigma-70, which promotes the attachment of the RNA polymerase to the DNA template strand at the promoter region. After the binding/initiation phase, RNA Polymerase sigma-70 holoenzyme catalyzes elongation, then like a caterpillar, the holoenzyme dies only to have a beautiful, strong, transcribing RNA Polymerase is born from the tattered shell of the holoenzyme. | First, regular RNA polymerase II binds to the sigma factor, sigma-70, which promotes the attachment of the RNA polymerase to the DNA template strand at the promoter region. After the binding/initiation phase, RNA Polymerase sigma-70 holoenzyme catalyzes elongation, then like a caterpillar, the holoenzyme dies only to have a beautiful, strong, transcribing RNA Polymerase is born from the tattered shell of the holoenzyme. | ||
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Highlighting the secondary structure of the RNA polymerase, <scene name='75/751191/Beta_sheets/1'>this scene shows the beta sheets in black.</scene> | Highlighting the secondary structure of the RNA polymerase, <scene name='75/751191/Beta_sheets/1'>this scene shows the beta sheets in black.</scene> | ||
| - | == Fun | + | == Fun Facts == |
Most studied bacterial RNA polymerase. | Most studied bacterial RNA polymerase. | ||
| - | + | Donald's favorite bacterial RNA polymerase. | |
Sigma factor 70 is the primary sigma factor of the E.coli. | Sigma factor 70 is the primary sigma factor of the E.coli. | ||
This is also two truths and a lie, you figure it out. | This is also two truths and a lie, you figure it out. | ||
| - | </StructureSection> | ||
Revision as of 22:53, 9 February 2017
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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Connor McDermott and Niall Cope's Structure:E.coli RNA Polymerase sigma-70 Holoenzyme
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Functions
First, regular RNA polymerase II binds to the sigma factor, sigma-70, which promotes the attachment of the RNA polymerase to the DNA template strand at the promoter region. After the binding/initiation phase, RNA Polymerase sigma-70 holoenzyme catalyzes elongation, then like a caterpillar, the holoenzyme dies only to have a beautiful, strong, transcribing RNA Polymerase is born from the tattered shell of the holoenzyme.
What it interacts with
The sigma factor alters the chemical structure of the RNA polymerase, allowing the RNA polyermase to bind to the promoter region, beginning elongation...so DNA I guess.
Where it Interacts
Since DNA is in the nucleus, and it interacts with DNA, I am gonna take a stab in the dark and say the golgi apparatus. No the interaction between the holoenzyme and the DNA happens in the nucleus.
What Organism is E.Coli RNA Polymerase Sigma-70 Holoenzyme located in?
E. Coli, so I guess.
Diseases
Lit bacterial infections like: cholecystitis, bactermia, cholangitis, UTIs, traveler's diarrhea (can strike at home), and meningitis.
Relevance
Pretty relevant to travelers, see [1]
Structural highlights
The RNA Polymerase Sigma-70 Holoenzyme has Highlighting the secondary structure of the RNA polymerase,
Fun Facts
Most studied bacterial RNA polymerase. Donald's favorite bacterial RNA polymerase. Sigma factor 70 is the primary sigma factor of the E.coli. This is also two truths and a lie, you figure it out.
