User:Kary Atkinson

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Example of backbone trace with ligand
 
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exercise 1
 
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<scene name='User:Kary_Atkinson/Glutamine_synthetase/2'>TextToBeDisplayed</scene>
 
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Ligand and Chain Selection With Labeling
 
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exercise 2
 
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<scene name='User:Kary_Atkinson/Glutamine_synthetase/5'>TextToBeDisplayed</scene>
 
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Active Site Residues
 
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exercise 3
 
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<scene name='User:Kary_Atkinson/Glutamine_synthetase/6'>TextToBeDisplayed</scene>
 
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Going Solo
 
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exercise 4
 
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<scene name='User:Kary_Atkinson/Glutamine_synthetase/7'>TextToBeDisplayed</scene>
 
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'''
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== Introduction ==
== Introduction ==
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Glutamine synthetase is composed of twelve subunits, formed as two hexameric rings. The two rings are held together by twelve central loops <insert wiki here showing the twelve central loops> which extend into the central region of the complex and include a small, four stranded β loop <insert wiki here showing β loops>. Each loop is 33 residues long and has a convex shape <insert wiki here showing a central loop between subunits>. The spatial orientation <insert wiki here showing the central cavity, loop orientation and distance between> of the loops has been found to be less accessible for interactions to occur, contributing to the catalytic activity of the enzyme.
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<applet scene='User:Kary_Atkinson/Pro_glutamine_synthetase/1' size='350' frame='true' align='right' caption='' />
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Glutamine synthetase is composed of twelve subunits, formed as two hexameric rings. The two rings are held together by twelve central loops <scene name='User:Kary_Atkinson/Pro_glutamine_synthetase/2'>TextToBeDisplayed</scene> which extend into the central region of the complex and include a small, four stranded β loop <scene name='User:Kary_Atkinson/Pro_glutamine_synthetase/3'>TextToBeDisplayed</scene>. Each loop is 33 residues long and has a convex shape. The spatial orientation <scene name='User:Kary_Atkinson/Pro_glutamine_synthetase/5'>TextToBeDisplayed</scene> of the loops has been found to be less accessible for interactions to occur, contributing to the catalytic activity of the enzyme.
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The central loop (residues 156-188) is a site where covalent modifications, with inhibitory effects are found. This segment of the complex is subject to proteolysis by four secreted proteases, which cleave specific residues. Another covalent modification known to occur at central loop of Glutamine synthetase is ADP-ribosylation of Arg-172 <scene name='User:Kary_Atkinson/Pro_glutamine_synthetase/12'>TextToBeDisplayed</scene>.
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It is evident then that the central loop of glutamine synthetase (residues 156-188) is an important component of the enzyme, anchoring the subunits together and providing the spatial orientation necessary for activity. Therefore the central loop contributes both to the function and stabilization, via numerous hydrophobic interactions <scene name='User:Kary_Atkinson/Pro_glutamine_synthetase/11'>TextToBeDisplayed</scene> and four different hydrogen bonding interactions <scene name='User:Kary_Atkinson/Pro_glutamine_synthetase/10'>TextToBeDisplayed</scene> of the quartenary structure of Glutamine synthetase.
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== References: ==
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'''1.''' Fisher, M. T., Stadtman, E. R., Oxidative Modification of Escherichia coli Glutamine Synthetase, The Journal of Biological Chemistry, 1992, Vol 267. No3, 1872-1880
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As all other enzymes, Glutamine synthetase contains an active site. However, unlike other enzymes it also contains a “passive site” known as the central loop (residues 156-188) where covalent modifications, with inhibitory effects are found. This segment of the complex is subject to proteolysis by four secreted proteases, which cleave specific residues <insert wiki here showing the cleavage sites> This characteristic is unique and exclusive to the central loop as no other glutamine synthetase sites away from the central loop are attacked, under the same mild conditions, by these enzymes. Another covalent modification known to occur at central loop of Glutamine synthetase is ADP-ribosylation of Arg-172 <insert wiki here showing the ADP-ribosylation site>.
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'''2.''' Moss, J., Stanley, S., Levine, R. L., Inactivation of Bacterial Glutamine Synthetase by ADP-ribosylation, The Journal of Biological Chemistry, 1990, Vol. 265, No. 34, 21056-21060
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It is evident then that the central loop of glutamine synthetase (residues 156-188) is an important component of the enzyme, anchoring the subunits together and providing the spatial orientation necessary for activity. Therefore the central loop contributes both to the function and stabilization, via numerous hydrophobic interactions <insert wiki here showing hydrophic interactions> and four different hydrogen bonding interactions <insert wiki here showing hydrogen bonds>, of the quartenary structure of Glutamine synthetase.
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'''3.''' Yamashita, M. M., Almassy, R. J., Janson, C. A., Cascio, D., Eisenberg, D., Refined Atomic Model of Glutamine Synthetase at 3.5 A Resolution, The Journal of Biochemistry, 1989, Vol. 264, No. 30, 17681-17690

Current revision

Introduction

Drag the structure with the mouse to rotate

Glutamine synthetase is composed of twelve subunits, formed as two hexameric rings. The two rings are held together by twelve central loops which extend into the central region of the complex and include a small, four stranded β loop . Each loop is 33 residues long and has a convex shape. The spatial orientation of the loops has been found to be less accessible for interactions to occur, contributing to the catalytic activity of the enzyme.


The central loop (residues 156-188) is a site where covalent modifications, with inhibitory effects are found. This segment of the complex is subject to proteolysis by four secreted proteases, which cleave specific residues. Another covalent modification known to occur at central loop of Glutamine synthetase is ADP-ribosylation of Arg-172 .


It is evident then that the central loop of glutamine synthetase (residues 156-188) is an important component of the enzyme, anchoring the subunits together and providing the spatial orientation necessary for activity. Therefore the central loop contributes both to the function and stabilization, via numerous hydrophobic interactions and four different hydrogen bonding interactions of the quartenary structure of Glutamine synthetase.



References:

1. Fisher, M. T., Stadtman, E. R., Oxidative Modification of Escherichia coli Glutamine Synthetase, The Journal of Biological Chemistry, 1992, Vol 267. No3, 1872-1880

2. Moss, J., Stanley, S., Levine, R. L., Inactivation of Bacterial Glutamine Synthetase by ADP-ribosylation, The Journal of Biological Chemistry, 1990, Vol. 265, No. 34, 21056-21060

3. Yamashita, M. M., Almassy, R. J., Janson, C. A., Cascio, D., Eisenberg, D., Refined Atomic Model of Glutamine Synthetase at 3.5 A Resolution, The Journal of Biochemistry, 1989, Vol. 264, No. 30, 17681-17690

Proteopedia Page Contributors and Editors (what is this?)

Kary Atkinson, Eran Hodis

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