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From Proteopedia

Revision as of 23:06, 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.

Connor McDermott and Niall Cope's Structure:E.coli RNA Polymerase sigma-70 Holoenzyme

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] and scroll down.

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.