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(Couple of sentences about the location of the complex and E. coli)
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== Function ==
== Function ==
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The sigma factor, Rpod, binds to the RNA polymerase in place of the alpha subunit. 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 ==
== Location ==
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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.
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== Relevance ==
== Relevance ==

Revision as of 22:24, 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.

Phe-tRNA, elongation factor EF-TU:GDPNP Ternary complex

Drag the structure with the mouse to rotate

Structure of E. coli Transcription Initiation Complex

Caption for this structure

Drag the structure with the mouse to rotate

References

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