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From Proteopedia
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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Taq Polymerase
Function
Taq polymerase is a DNA polymerase, an enzyme that synthesizes DNA by adding nucleotides onto a growing nucleic acid. It has the ability to withstand temperatures of over 90 degrees Celsius; its ability to function in extreme heat makes it a useful tool for PCR. Taq polymerase is structurally similar to DNA Polymerase I (Pol I) from E. coli, but lacks Pol I's exonuclease activity, and is thus unable to proofread the DNA it synthesizes.
What it interacts with
Taq polymerase interacts with free-floating DNA nucleotides, scooping them up and synthesizing them into a strand of DNA. It attaches to the minor groove of the DNA helix.
Where it interacts
On the molecule itself, the primary interaction is carried out at the active site, the structure of which enables the linkage of the DNA nucleotides. In the cell, the molecule floats around the cytoplasm, and binds to a strand of DNA when it starts connecting the nucleotides.
Origins
Taq polymerase can be found in the extremophilic bacterium Thermus aquaticus. The bacterium lives in conditions that are very hot (50 to 80 degrees Celsius), so it requires a DNA polymerase that functions in high temperatures. This polymerase was isolated by Chien et al. in 1976.
Structural highlights
The most important part of any protein is the structure that holds everything together: . The backbone runs through the protein's larger structure, allowing the other parts to perform their respective function.
The main function of the molecule, of course, is to construct (green). The DNA runs through the active site of the molecule, and is built upon.
The (blue) are necessary to perform this function as well. They attach onto the protein, changing its overall conformation, allowing it to become the shape that it needs to be in order to properly construct DNA.
