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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

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E.coli Pol II-normal DNA-dGTP ternary complex

E.coli DNA Pol II

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Function

Involved in DNA repair and/or mutagenesis. Its molecular functions include:

  • Nucleotide Binding
  • 3' to 5' exodeoxyribonuclease activity
  • 3' to 5' exonuclease activity
  • Transferase Activity
  • Nucleotidyltransferase activity

Interactions

  • On a molecular level, it interacts with mismatched base pairs at its active site and the exonuclease site.
  • On a cellular level Interacts with damaged or mismatched sites on the DNA, in the nucleoid of a cell.

Origins

Found in Prokaryotes, specifically in E.coli encoded by the b0060, dinA, JW0059, polB genes.


Structural highlights

The (highlighted in black) of Ecoli Pol II which plays an important role in its structure The structure of E.Coli Pol II is highlighted in red. The are highlighted in blue. </StructureSection>

References

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