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==Function==
==Function==
<StructureSection load='1tau' size='340' side='right' caption='lookit' scene=''>
<StructureSection load='1tau' size='340' side='right' caption='lookit' scene=''>
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A polymerase is an enzyme that adds nucleotides onto a growing nucleic acid. Taq polymerase is a DNA polymerase that can be found in T. aquaticus, a bacterium that lives in very hot conditions. Taq polymerase has the ability to withstand temperatures of 75 to 80 degrees Celcius, so it can perform its function in the environment that T. aquaticus lives in.
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A polymerase is an enzyme that adds nucleotides onto a growing nucleic acid. Taq polymerase is a DNA polymerase Taq polymerase has the ability to withstand temperatures of 75 to 80 degrees Celcius, so it can perform its function in extreme conditions.
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== Relevance ==
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== What it interacts with ==
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The molecule interacts with freefloating DNA nucleotides, scooping them up and combining them into a strand of DNA.
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== Where it interacts ==
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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.
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== Where it originates ==
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Taq polymerase can be found in the extremophilic bacterium Thermus aquaticus. The bacterium lives in conditions that are very hot (75 to 80 degrees Celsius), so it requires a DNA polymerase that can function in high temperatures.
== Structural highlights ==
== Structural highlights ==
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</StructureSection>
</StructureSection>
== References ==
== References ==
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https://en.wikipedia.org/wiki/Taq_polymerase
<references/>
<references/>

Revision as of 20:57, 8 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

Taq Polymerase

Function

lookit

Drag the structure with the mouse to rotate

References

https://en.wikipedia.org/wiki/Taq_polymerase

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