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DNA Origami Assembly for the Tar Chemoreceptor: Difference between revisions

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==Your Heading Here (maybe something like 'Structure')==
==DNA Origami as an Assembly Method for Tar Chemoreceptor==
<StructureSection load='3ja6' size='340' side='right' caption='DNA Origami Chemoreceptor complex' scene=''>
<StructureSection load='3ja6' size='340' side='right' caption='DNA Origami Chemoreceptor complex' scene=''>
This is a default text for your page '''DNA Origami Assembly for the Tar Chemoreceptor'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
 
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
This project centers around the idea of using DNA origami to assemble the Tar chemoreceptor. This assembly method would provide novel opportunities to investigate how this receptor works previously untestable using other assembly methods
 
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref>  


== Introduction to Chemotaxis ==
== Introduction to Chemotaxis ==
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== DNA Origami ==
== DNA Origami ==
This project involves using a DNA tetrahedron as a scaffold for the Tar chemoreceptor complex ''in vitro''. In this model, receptor dimers are attached at three vertices of the DNA tetrahedron to make the native trimer of dimers structure seen ''in vivo''. At the other end of the receptor, two proteins are shown: CheA, a kinase, shown in dark blue, and CheW, a coupling protein, shown in cyan.  
This project involves using a DNA tetrahedron as a scaffold for the Tar chemoreceptor complex ''in vitro''. In this model, receptor dimers are attached at three vertices of the DNA tetrahedron to make the native <scene name='80/800127/Entire_trimer_of_dimers/2'>trimer of dimers</scene> structure seen ''in vivo''. At the other end of the receptor, two proteins are shown: CheA, a kinase and CheW, a coupling protein.  
 
<scene name='80/800127/Entire_trimer_of_dimers/2'>trimer of dimers</scene>


==Attachment to DNA==
==Attachment to DNA==
The protein receptor dimer is attached to the DNA tetrahedron using NTA-functionalized DNA. This means that the DNA has an NTA, or nitrilotriaceticacid, is able to coordinate with nickel ions, shown in green, which is also able to coordinate with histidines. The Tar chemoreceptor has six histidines added to the N-terminus of the protein ''in vitro'', which should be able to coordinate with the nickel ion as well, creating a coordination complex.
The protein receptor dimer is <scene name='80/800127/Zoomed_in_connection/1'>attached to the DNA tetrahedron</scene> using NTA-functionalized DNA. This means that the DNA has an NTA, or nitrilotriaceticacid, is able to coordinate with nickel ions, shown in green, which is also able to coordinate with histidines. The Tar chemoreceptor has six histidines added to the N-terminus of the protein ''in vitro'', which should be able to coordinate with the nickel ion as well, creating a coordination complex.  
 
<scene name='80/800127/Zoomed_in_connection/1'>DNA-protein linkage</scene>
 
== Structural highlights ==
 
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.


</StructureSection>
</StructureSection>
== References ==
== References ==
<references/>
<references/>

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Dominique Kiki Carey, Michal Harel
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