Sandbox Reserved 1293
From Proteopedia
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== Location == | == 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. | 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 | + | |
+ | == Interactions between the DNA, RNA Polymerase, and Sigma Factor == | ||
+ | |||
+ | <scene name='75/751186/Dna-complex_interaction/1'>TextToBeDisplayed</scene> | ||
== Structural highlights == | == Structural highlights == |
Revision as of 23:11, 9 February 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 of E. coli Transcription Initiation Complex
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