Sandbox Reserved 1293
From Proteopedia
(first sentence on structure) |
|||
| Line 2: | Line 2: | ||
==Structure of E. coli Transcription Initiation Complex== | ==Structure of E. coli Transcription Initiation Complex== | ||
<StructureSection load='4yln' size='340' side='right' caption='Caption for this structure' scene=''> | <StructureSection load='4yln' size='340' side='right' caption='Caption for this structure' scene=''> | ||
| - | This is a 27 chain protein structure with 11244 amino acid alpha carbons. | ||
| - | == Function == | ||
| - | == | + | == Function == |
| + | The sigma factor allows the initiation complex to bind to the consensus -25 sequence which positions the RNA polymerase above the start site. RNA polymerase then undergoes morphological changes to fit to the DNA. This change in shape permits the sigma factor to escape before the RNA polymerase starts abortive transcription. After abortive transcription, the RNA polymerase can begin transcribing the DNA sequence. | ||
| - | == | + | == Interactions between the RNA polymerase, sigma factor, and DNA sequence == |
| + | == Organism == | ||
| + | This is the initiation complex within E. coli, thus the information on this page pertains to prokaryotic transcription | ||
== Structural highlights == | == Structural highlights == | ||
Revision as of 21:47, 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.
| |||||||||||
Structure of E. coli Transcription Initiation Complex
| |||||||||||
