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Human Glutamine Synthetase Tertiary Structure: Pfam domains
<applet load='2ktq.pdb' size='300' frame='true' align='right' caption='Klentaq1–Open conformation' scene= 'Sandbox_dvoet/DNA_polymerase/Klentaq1-open_conformation/2'/>


The active site of Glutamine synthetase is the result of the interactions between two adjacent subunits.
Here, Klentaq1's N-terminal, palm, fingers and thumb domains are yellow, magenta, green, and blue, respectively. The DNA is drawn in stick form colored according to atom type (template C cyan, primer C green, N blue, O red, and P orange). The primer's 3' ddC residue is shown in space-filling form as is the bound ddCTP, in which is C yellow.
Each Subunits contains two two ends, the C-terminus and the N-terminus. The Glutamine synthetase beta grasp domain(N-terminus), and the Glutamine synthetase catalytic domain (the C-terminus). In order to stabilize the molecule, the two domains are involved in the Van Der Walls , Hydrogen . The Beta Grasp  domain interact with the C-terminus of the next subunit.the two domains are proceeded by a meander of 3-24 residues that link the chains in the proteins core.  


Beta Grasp domain (N-terminus)
-comprised of residues 43-123
-binds glutamate, ammonia, and ATP
<show protein alignment image>
<show structure of the domain in viewer>


Catalytic domain (C-terminus)
-comprised of residues 129-382
-how it functions is not described, more research is necessary here


<show alignment image>
<show structure of the domain in viewer>


Active site
<scene name='Sandbox_dvoet/DNA_polymerase/Morphtest1/1'>morph test scene</scene>
-there are 10 active sites in the decamer of the protein, each formed from the beta grasp domain of one chain and the catalytic domain of the neighboring chain.
<show relation between chains, domains, and active sites with viewer>
-describe visually the important aspects of the active site
<show active site and ligands relationship, may need multiple scenes>
 
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Revision as of 17:04, 19 November 2009

Klentaq1–Open conformation

Drag the structure with the mouse to rotate

Here, Klentaq1's N-terminal, palm, fingers and thumb domains are yellow, magenta, green, and blue, respectively. The DNA is drawn in stick form colored according to atom type (template C cyan, primer C green, N blue, O red, and P orange). The primer's 3' ddC residue is shown in space-filling form as is the bound ddCTP, in which is C yellow.



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