Proteopedia - User contributions [en]

User talk:Adrian Aldrich/Prokaryotic Glutamine Synthetase Pfam Domains

2008-12-20T04:20:53Z

Adrian Aldrich:

{{STRUCTURE_1lgr | PDB=1lgr | SCENE= }}
'''Prokaryotic Glutamine Synthetase Tertiary Structure: PFam domains'''

Prokaryotic Glutamine Synthetase[http://en.wikipedia.org/wiki/Glutamine_synthetase] is a dodecamer, comprised of 12 identical polypeptide chains, organized as a dimer of two disk like hexamers. Each protomer contains 2 Pfam[http://en.wikipedia.org/wiki/Pfam] domains, the Beta-grasp domain and the catalytic domain, preceded at the N terminus by short chains(3-13)of resides which link the all protomers together in the dodecamers core.

'''Beta Grasp domain'''

The <scene name='User:Adrian_Aldrich/Prokaryotic_Glutamine_Synthetase_Pfam_Domains_Outline/Betagrasp/1'>Beta-Grasp Domain</scene> is the N-terminal domain, extending from residues 13-94. This domain is responsible for binding ATP[http://en.wikipedia.org/wiki/Adenosine_triphosphate], Glutamate[http://en.wikipedia.org/wiki/Glutamate], and Ammonia[http://en.wikipedia.org/wiki/Amonia]. The domain folds into a bent beta-sheet[http://en.wikipedia.org/wiki/Beta_sheet] flanked by two short alpha helices[http://en.wikipedia.org/wiki/Alpha_helices], forming a pocket for the ligands to bind. ATP[http://en.wikipedia.org/wiki/Adenosine_triphosphate] binds first, activating the site for binding glutamate.

'''Catalytic domain'''

The <scene name='User:Adrian_Aldrich/Prokaryotic_Glutamine_Synthetase_Pfam_Domains_Outline/Catalytic/1'>Catalytic Domain</scene> is the C-terminal domain, extending from residues 101-382, and forms a melon rind shaped thin beta sheet[http://en.wikipedia.org/wiki/Beta_sheet] coated on one side by several alpha helices[http://en.wikipedia.org/wiki/Alpha_helices].

'''Active site'''

The dodecamer contains 12 <scene name='User:Adrian_Aldrich/Prokaryotic_Glutamine_Synthetase_Pfam_Domains_Outline/Active_site/1'> Active sites</scene> in total, each formed from the Beta-grasp domain of one protomer and the Catalytic domain of the neighboring protomer. The concave beta sheet of the Catalytic domain( in green ) faces the pocket of the neighboring Beta-grasp domain( in red ), creating a funnel shaped hollow in which binding and catalysis is performed.

User talk:Adrian Aldrich/Prokaryotic Glutamine Synthetase Pfam Domains

2008-12-20T04:20:04Z

Adrian Aldrich:

{{STRUCTURE_1lgr | PDB=1lgr | SCENE= }}
'''Prokaryotic Glutamine Synthetase Tertiary Structure: PFam domains'''

Prokaryotic Glutamine Synthetase[[Glutamine Synthetase|Glutamine Synthetase]][http://en.wikipedia.org/wiki/Glutamine_synthetase] is a dodecamer, comprised of 12 identical polypeptide chains, organized as a dimer of two disk like hexamers. Each protomer contains 2 Pfam[http://en.wikipedia.org/wiki/Pfam] domains, the Beta-grasp domain and the catalytic domain, preceded at the N terminus by short chains(3-13)of resides which link the all protomers together in the dodecamers core.

'''Beta Grasp domain'''

The <scene name='User:Adrian_Aldrich/Prokaryotic_Glutamine_Synthetase_Pfam_Domains_Outline/Betagrasp/1'>Beta-Grasp Domain</scene> is the N-terminal domain, extending from residues 13-94. This domain is responsible for binding ATP[http://en.wikipedia.org/wiki/Adenosine_triphosphate], Glutamate[http://en.wikipedia.org/wiki/Glutamate], and Ammonia[http://en.wikipedia.org/wiki/Amonia]. The domain folds into a bent beta-sheet[http://en.wikipedia.org/wiki/Beta_sheet] flanked by two short alpha helices[http://en.wikipedia.org/wiki/Alpha_helices], forming a pocket for the ligands to bind. ATP[http://en.wikipedia.org/wiki/Adenosine_triphosphate] binds first, activating the site for binding glutamate.

'''Catalytic domain'''

The <scene name='User:Adrian_Aldrich/Prokaryotic_Glutamine_Synthetase_Pfam_Domains_Outline/Catalytic/1'>Catalytic Domain</scene> is the C-terminal domain, extending from residues 101-382, and forms a melon rind shaped thin beta sheet[http://en.wikipedia.org/wiki/Beta_sheet] coated on one side by several alpha helices[http://en.wikipedia.org/wiki/Alpha_helices].

'''Active site'''

The dodecamer contains 12 <scene name='User:Adrian_Aldrich/Prokaryotic_Glutamine_Synthetase_Pfam_Domains_Outline/Active_site/1'> Active sites</scene> in total, each formed from the Beta-grasp domain of one protomer and the Catalytic domain of the neighboring protomer. The concave beta sheet of the Catalytic domain( in green ) faces the pocket of the neighboring Beta-grasp domain( in red ), creating a funnel shaped hollow in which binding and catalysis is performed.

User talk:Adrian Aldrich/Prokaryotic Glutamine Synthetase Pfam Domains

2008-12-19T22:33:23Z

Adrian Aldrich:

User talk:Adrian Aldrich/Prokaryotic Glutamine Synthetase Pfam Domains

2008-12-19T22:28:38Z

Adrian Aldrich:

{{STRUCTURE_1lgr | PDB=1lgr | SCENE= }}
'''Prokaryotic Glutamine Synthetase Tertiary Structure: PFam domains'''

Prokaryotic Glutamine Synthetase[http://en.wikipedia.org/wiki/Glutamine_synthetase] is a dodecamer, comprised of 12 identical polypeptide chains, organized as a dimer of two disk like hexamers. Each protomer contains 2 Pfam[http://en.wikipedia.org/wiki/Pfam] domains, the Beta-grasp domain and the catalytic domain, preceded at the N terminus by short chains(3-13)of resides which link the all protomers together in the dodecamers core.

'''Beta Grasp domain'''

The <scene name='User:Adrian_Aldrich/Prokaryotic_Glutamine_Synthetase_Pfam_Domains_Outline/Betagrasp/1'>Beta-Grasp Domain</scene> is the N-terminal domain, extending from residues 13-94. This domain is responsible for binding ATP[http://en.wikipedia.org/wiki/Adenosine_triphosphate], Glutamate[http://en.wikipedia.org/wiki/Glutamate], and Ammonia[http://en.wikipedia.org/wiki/Amonia]. The domain folds into a bent beta-sheet[http://en.wikipedia.org/wiki/Beta_sheet] flanked by two short alpha helices[http://en.wikipedia.org/wiki/Alpha_helices], forming a pocket for the ligands to bind. ATP[http://en.wikipedia.org/wiki/Adenosine_triphosphate] binds first, activating the site for binding glutamate.

'''Catalytic domain'''

The <scene name='User:Adrian_Aldrich/Prokaryotic_Glutamine_Synthetase_Pfam_Domains_Outline/Catalytic/1'>Catalytic Domain</scene> is the C-terminal domain, extending from residues 101-382, and forms a melon rind shaped thin beta sheet coated on one side by several alpha helices.

'''Active site'''

The dodecamer contains 12 <scene name='User:Adrian_Aldrich/Prokaryotic_Glutamine_Synthetase_Pfam_Domains_Outline/Active_site/1'> Active sites</scene> in total, each formed from the Beta-grasp domain of one protomer and the Catalytic domain of the neighboring protomer. The concave beta sheet of the Catalytic domain( in green ) faces the pocket of the neighboring Beta-grasp domain( in red ), creating a funnel shaped hollow in which binding and catalysis is performed.

User talk:Adrian Aldrich/Prokaryotic Glutamine Synthetase Pfam Domains

2008-12-19T22:23:31Z

Adrian Aldrich:

{{STRUCTURE_1lgr | PDB=1lgr | SCENE= }}
'''Prokaryotic Glutamine Synthetase Tertiary Structure: PFam domains'''

Prokaryotic Glutamine Synthetase[http://en.wikipedia.org/wiki/Glutamine_synthetase] is a dodecamer, comprised of 12 identical polypeptide chains, organized as a dimer of two disk like hexamers. Each protomer contains 2 Pfam[http://en.wikipedia.org/wiki/Pfam] domains, the Beta-grasp domain and the catalytic domain, preceded at the N terminus by short chains(3-13)of resides which link the all protomers together in the dodecamers core.

'''Beta Grasp domain'''

The <scene name='User:Adrian_Aldrich/Prokaryotic_Glutamine_Synthetase_Pfam_Domains_Outline/Betagrasp/1'>Beta-Grasp Domain</scene> is the N-terminal domain, extending from residues 13-94. This domain is responsible for binding ATP, Glutamate, and Ammonia. The domain folds into a bent beta-sheet flanked by two short alpha helices, forming a pocket for the ligands to bind. ATP binds first, activating the site for binding glutamate.

'''Catalytic domain'''

The <scene name='User:Adrian_Aldrich/Prokaryotic_Glutamine_Synthetase_Pfam_Domains_Outline/Catalytic/1'>Catalytic Domain</scene> is the C-terminal domain, extending from residues 101-382, and forms a melon rind shaped thin beta sheet coated on one side by several alpha helices.

'''Active site'''

The dodecamer contains 12 <scene name='User:Adrian_Aldrich/Prokaryotic_Glutamine_Synthetase_Pfam_Domains_Outline/Active_site/1'> Active sites</scene> in total, each formed from the Beta-grasp domain of one protomer and the Catalytic domain of the neighboring protomer. The concave beta sheet of the Catalytic domain( in green ) faces the pocket of the neighboring Beta-grasp domain( in red ), creating a funnel shaped hollow in which binding and catalysis is performed.

User talk:Adrian Aldrich/Prokaryotic Glutamine Synthetase Pfam Domains

2008-12-19T22:18:19Z

Adrian Aldrich:

{{STRUCTURE_1lgr | PDB=1lgr | SCENE= }}
'''Prokaryotic Glutamine Synthetase Tertiary Structure: PFam domains'''

Prokaryotic Glutamine Synthetase[http://en.wikipedia.org/wiki/Glutamine_synthetase] is a dodecamer, comprised of 12 identical polypeptide chains, organized as a dimer of two disk like hexamers. Each protomer contains 2 Pfam domains, the Beta-grasp domain and the catalytic domain, preceded at the N terminus by short chains(3-13)of resides which link the all protomers together in the dodecamers core.

'''Beta Grasp domain'''

The <scene name='User:Adrian_Aldrich/Prokaryotic_Glutamine_Synthetase_Pfam_Domains_Outline/Betagrasp/1'>Beta-Grasp Domain</scene> is the N-terminal domain, extending from residues 13-94. This domain is responsible for binding ATP, Glutamate, and Ammonia. The domain folds into a bent beta-sheet flanked by two short alpha helices, forming a pocket for the ligands to bind. ATP binds first, activating the site for binding glutamate.

'''Catalytic domain'''

The <scene name='User:Adrian_Aldrich/Prokaryotic_Glutamine_Synthetase_Pfam_Domains_Outline/Catalytic/1'>Catalytic Domain</scene> is the C-terminal domain, extending from residues 101-382, and forms a melon rind shaped thin beta sheet coated on one side by several alpha helices.

'''Active site'''

The dodecamer contains 12 <scene name='User:Adrian_Aldrich/Prokaryotic_Glutamine_Synthetase_Pfam_Domains_Outline/Active_site/1'> Active sites</scene> in total, each formed from the Beta-grasp domain of one protomer and the Catalytic domain of the neighboring protomer. The concave beta sheet of the Catalytic domain( in green ) faces the pocket of the neighboring Beta-grasp domain( in red ), creating a funnel shaped hollow in which binding and catalysis is performed.

User:Adrian Aldrich

2008-12-17T00:45:31Z

Adrian Aldrich:

I am a student at the University of Maryland.
If you are looking for the assignment due 11/24/08 please go to...
http://www.proteopedia.org/wiki/index.php/User:Adrian_Aldrich/Section_1
For the outline of our cotribution to the prokaryotic glutamine synthetase page go to...
http://www.proteopedia.org/wiki/index.php/User:Adrian_Aldrich/Prokaryotic_Glutamine_Synthetase_Pfam_Domains_Outline
For the final version of the class project wiki please see.... http://www.proteopedia.org/wiki/index.php/User_talk:Adrian_Aldrich/Prokaryotic_Glutamine_Synthetase_Pfam_Domains

User talk:Adrian Aldrich/Prokaryotic Glutamine Synthetase Pfam Domains

2008-12-17T00:44:05Z

Adrian Aldrich: New page: {{STRUCTURE_1lgr | PDB=1lgr | SCENE= }} '''Prokaryotic Glutamine Synthetase Tertiary Structure: PFam domains''' Prokaryotic Glutamine Synthetase is a dodecamer, comprised of 12 identi...

{{STRUCTURE_1lgr | PDB=1lgr | SCENE= }}
'''Prokaryotic Glutamine Synthetase Tertiary Structure: PFam domains'''

Prokaryotic Glutamine Synthetase is a dodecamer, comprised of 12 identical polypeptide chains, organized as a dimer of two disk like hexamers. Each protomer contains 2 Pfam domains, the Beta-grasp domain and the catalytic domain, preceded at the N terminus by short chains(3-13)of resides which link the all protomers together in the dodecamers core.

'''Beta Grasp domain'''

The <scene name='User:Adrian_Aldrich/Prokaryotic_Glutamine_Synthetase_Pfam_Domains_Outline/Betagrasp/1'>Beta-Grasp Domain</scene> is the N-terminal domain, extending from residues 13-94. This domain is responsible for binding ATP, Glutamate, and Ammonia. The domain folds into a bent beta-sheet flanked by two short alpha helices, forming a pocket for the ligands to bind. ATP binds first, activating the site for binding glutamate.

'''Catalytic domain'''

The <scene name='User:Adrian_Aldrich/Prokaryotic_Glutamine_Synthetase_Pfam_Domains_Outline/Catalytic/1'>Catalytic Domain</scene> is the C-terminal domain, extending from residues 101-382, and forms a melon rind shaped thin beta sheet coated on one side by several alpha helices.

'''Active site'''

The dodecamer contains 12 <scene name='User:Adrian_Aldrich/Prokaryotic_Glutamine_Synthetase_Pfam_Domains_Outline/Active_site/1'> Active sites</scene> in total, each formed from the Beta-grasp domain of one protomer and the Catalytic domain of the neighboring protomer. The concave beta sheet of the Catalytic domain( in green ) faces the pocket of the neighboring Beta-grasp domain( in red ), creating a funnel shaped hollow in which binding and catalysis is performed.

User:Adrian Aldrich/Prokaryotic Glutamine Synthetase Pfam Domains Outline

2008-12-17T00:42:01Z

Adrian Aldrich:

User:Adrian Aldrich/Prokaryotic Glutamine Synthetase Pfam Domains Outline

2008-12-17T00:36:09Z

Adrian Aldrich:

User:Adrian Aldrich/Prokaryotic Glutamine Synthetase Pfam Domains Outline

2008-12-17T00:31:39Z

Adrian Aldrich:

{{STRUCTURE_1lgr | PDB=1lgr | SCENE= }}
'''Prokaryotic Glutamine Synthetase Tertiary Structure: PFam domains'''

Prokaryotic Glutamine Synthetase is a dodecamer, comprised of 12 identical polypeptide chains, organized as a dimer of two disk like hexamers. Each protomer contains 2 Pfam domains, the Beta-grasp domain and the catalytic domain, preceded at the N terminus by short chains(3-13)of resides which link the all protomers together in the dodecamers core.

'''Beta Grasp domain'''

The <scene name='User:Adrian_Aldrich/Prokaryotic_Glutamine_Synthetase_Pfam_Domains_Outline/Betagrasp/1'>Beta-Grasp Domain</scene> is the N-terminal domain, extending from residues 13-94. This domain is responsible for binding ATP, Glutamate, and Ammonia. The domain folds into a bent beta-sheet flanked by two short alpha helices, forming a pocket for the ligands to bind. ATP binds first, activating the site for binding glutamate.

'''Catalytic domain'''

The <scene name='User:Adrian_Aldrich/Prokaryotic_Glutamine_Synthetase_Pfam_Domains_Outline/Catalytic/1'>Catalytic Domain</scene> is the C-terminal domain, extending from residues 101-382.

'''Active site'''

The dodecamer contains 12 <scene name='User:Adrian_Aldrich/Prokaryotic_Glutamine_Synthetase_Pfam_Domains_Outline/Active_site/1'> Active sites</scene> in total, each formed from the Beta-grasp domain of one protomer and the Catalytic domain of the neighboring protomer.

User:Adrian Aldrich/Prokaryotic Glutamine Synthetase Pfam Domains Outline

2008-12-17T00:29:38Z

Adrian Aldrich:

{{STRUCTURE_1lgr | PDB=1lgr | SCENE= }}
'''Prokaryotic Glutamine Synthetase Tertiary Structure: PFam domains'''

Prokaryotic Glutamine Synthetase is a dodecamer, comprised of 12 identical polypeptide chains, organized as a dimer of two disk like hexamers. Each protomer contains 2 Pfam domains, the Beta-grasp domain and the catalytic domain, preceded at the N terminus by short chains(3-13)of resides which link the all protomers together in the dodecamers core.

'''Beta Grasp domain'''

The <scene name='User:Adrian_Aldrich/Prokaryotic_Glutamine_Synthetase_Pfam_Domains_Outline/Betagrasp/1'>Beta-Grasp Domain</scene> is the N-terminal domain, extending from residues 13-94. This domain is responsible for binding ATP, Glutamate, and Ammonia. The domain folds into a bent beta-sheet flanked by two short alpha helices, forming a pocket for the ligands to bind. ATP binds first, activating the site for binding glutamate.
<scene name='User:Adrian_Aldrich/Prokaryotic_Glutamine_Synthetase_Pfam_Domains_Outline/Betagrasp/1'>Prokaryotic Glutamine Synthetase Beta-Grasp Domain</scene>

'''Catalytic domain'''

The catalytic domain is the C-terminal domain, extending from residues 101-382.
<scene name='User:Adrian_Aldrich/Prokaryotic_Glutamine_Synthetase_Pfam_Domains_Outline/Catalytic/1'>Prokaryotic Glutamine Synthetase Catalytic Domain</scene>

'''Active site'''

The dodecamer contains 12 active sites total, each formed from the Beta-grasp domain of one protomer and the Catalytic domain of the neighboring protomer.
<scene name='User:Adrian_Aldrich/Prokaryotic_Glutamine_Synthetase_Pfam_Domains_Outline/Active_site/1'>Prokaryotic Glutamine Synthetase Active site</scene>

User:Adrian Aldrich/Prokaryotic Glutamine Synthetase Pfam Domains Outline

2008-12-17T00:22:47Z

Adrian Aldrich:

{{STRUCTURE_1lgr | PDB=1lgr | SCENE= }}
'''Prokaryotic Glutamine Synthetase Tertiary Structure: PFam domains'''

Prokaryotic Glutamine Synthetase is a dodecamer, comprised of 12 identical polypeptide chains, organized as a dimer of two disk like hexamers. Each protomer contains 2 Pfam domains, the Beta-grasp domain and the catalytic domain, preceded at the N terminus by short chains(3-13)of resides which link the all protomers together in the dodecamers core.

'''Beta Grasp domain'''

The Beta-grasp domain is the N-terminal domain, extending from residues 13-94. This domain is responsible for binding ATP, Glutamate, and Ammonia. ATP binds first, activating the site for binding glutamate.
<scene name='User:Adrian_Aldrich/Prokaryotic_Glutamine_Synthetase_Pfam_Domains_Outline/Betagrasp/1'>Prokaryotic Glutamine Synthetase Beta-Grasp Domain</scene>

'''Catalytic domain'''

The catalytic domain is the C-terminal domain, extending from residues 101-382.
<scene name='User:Adrian_Aldrich/Prokaryotic_Glutamine_Synthetase_Pfam_Domains_Outline/Catalytic/1'>Prokaryotic Glutamine Synthetase Catalytic Domain</scene>

'''Active site'''

The dodecamer contains 12 active sites total, each formed from the Beta-grasp domain of one protomer and the Catalytic domain of the neighboring protomer.
<scene name='User:Adrian_Aldrich/Prokaryotic_Glutamine_Synthetase_Pfam_Domains_Outline/Active_site/1'>Prokaryotic Glutamine Synthetase Active site</scene>

User:Adrian Aldrich/Prokaryotic Glutamine Synthetase Pfam Domains Outline

2008-12-16T23:41:08Z

Adrian Aldrich:

'''Prokaryotic Glutamine Synthetase Tertiary Structure: PFam domains'''
{{STRUCTURE_1lgr | PDB=1lgr | SCENE= }}

Prokaryotic Glutamine Synthetase is a dodecamer, comprised of 12 identical polypeptide chains, organized as a dimer of two disk like hexamers. Each protomer contains 2 Pfam domains, the Beta Grasp domain and the catalytic domain, preceded by meanders of a few resides in length which link the protomers together in the dodecamers core.

'''Beta Grasp domain'''

The beta grasp domain is the N-terminal domain, extending from residues 13-94. This domain is responsible for binding ATP, Glutamate, and Ammonia. ATP binds first, activating the site for binding glutamate.
<scene name='User:Adrian_Aldrich/Prokaryotic_Glutamine_Synthetase_Pfam_Domains_Outline/Betagrasp/1'>Prokaryotic Glutamine Synthetase Beta-Grasp Domain</scene>

'''Catalytic domain'''

The catalytic domain is the C-terminal domain, extending from residues 101-382.
<scene name='User:Adrian_Aldrich/Prokaryotic_Glutamine_Synthetase_Pfam_Domains_Outline/Catalytic/1'>Prokaryotic Glutamine Synthetase Catalytic Domain</scene>

'''Active site'''

The dodecamer contains 12 active sites total, each formed from the Beta grasp domain of one protomer and the Catalytic domain of the neighboring protomer.
<scene name='User:Adrian_Aldrich/Prokaryotic_Glutamine_Synthetase_Pfam_Domains_Outline/Active_site/1'>Prokaryotic Glutamine Synthetase Active site</scene>

User:Adrian Aldrich/Prokaryotic Glutamine Synthetase Pfam Domains Outline

2008-12-16T23:38:47Z

Adrian Aldrich:

'''Prokaryotic Glutamine Synthetase Tertiary Structure: PFam domains'''
{{STRUCTURE_1lgr | PDB=1lgr | SCENE= }}

Prokaryotic Glutamine Synthetase is a dodecamer, comprised of 12 identical polypeptide chains, organized as a dimer of two disk like hexamers. Each protomer contains 2 Pfam domains, the Beta Grasp domain and the catalytic domain, preceded by meanders of a few resides in length which link the protomers together in the dodecamers core.

'''Beta Grasp domain'''

The beta grasp domain is the N-terminal domain, extending from residues 13-94. This domain is responsible for binding ATP, Glutamate, and Ammonia. ATP binds first, activating the site for binding glutamate.
<scene name='User:Adrian_Aldrich/Prokaryotic_Glutamine_Synthetase_Pfam_Domains_Outline/Betagrasp/1'>Prokaryotic Glutamine Synthetase Beta-Grasp Domain</scene>

'''Catalytic domain'''

The catalytic domain is the C-terminal domain, extending from residues 101-382.
<applet load='Catalytic' size='300' frame='true' align='right' caption='The Prokaryotic Glutamine Synthetase Catalytic Domain' />

'''Active site'''

The dodecamer contains 12 active sites total, each formed from the Beta grasp domain of one protomer and the Catalytic domain of the neighboring protomer.
<applet load='Active_site' size='300' frame='true' align='right' caption='Insert caption here' />

User:Adrian Aldrich/Prokaryotic Glutamine Synthetase Pfam Domains Outline

2008-12-16T23:37:51Z

Adrian Aldrich:

'''Prokaryotic Glutamine Synthetase Tertiary Structure: PFam domains'''

Prokaryotic Glutamine Synthetase is a dodecamer, comprised of 12 identical polypeptide chains, organized as a dimer of two disk like hexamers. Each protomer contains 2 Pfam domains, the Beta Grasp domain and the catalytic domain, preceded by meanders of a few resides in length which link the protomers together in the dodecamers core.

'''Beta Grasp domain'''

The beta grasp domain is the N-terminal domain, extending from residues 13-94. This domain is responsible for binding ATP, Glutamate, and Ammonia. ATP binds first, activating the site for binding glutamate.
<scene name='User:Adrian_Aldrich/Prokaryotic_Glutamine_Synthetase_Pfam_Domains_Outline/Betagrasp/1'>Prokaryotic Glutamine Synthetase Beta-Grasp Domain</scene>

'''Catalytic domain'''

The catalytic domain is the C-terminal domain, extending from residues 101-382.
<applet load='Catalytic' size='300' frame='true' align='right' caption='The Prokaryotic Glutamine Synthetase Catalytic Domain' />

'''Active site'''

The dodecamer contains 12 active sites total, each formed from the Beta grasp domain of one protomer and the Catalytic domain of the neighboring protomer.
<applet load='Active_site' size='300' frame='true' align='right' caption='Insert caption here' />

{{STRUCTURE_1lgr | PDB=1lgr | SCENE= }}

User:Adrian Aldrich/Prokaryotic Glutamine Synthetase Pfam Domains Outline

2008-12-16T23:35:17Z

Adrian Aldrich:

'''Prokaryotic Glutamine Synthetase Tertiary Structure: PFam domains'''

Prokaryotic Glutamine Synthetase is a dodecamer, comprised of 12 identical polypeptide chains, organized as a dimer of two disk like hexamers. Each protomer contains 2 Pfam domains, the Beta Grasp domain and the catalytic domain, preceded by meanders of a few resides in length which link the protomers together in the dodecamers core.

'''Beta Grasp domain'''

The beta grasp domain is the N-terminal domain, extending from residues 13-94. This domain is responsible for binding ATP, Glutamate, and Ammonia. ATP binds first, activating the site for binding glutamate.
<applet load='Betagrasp' size='300' frame='true' align='right' caption='The Prokaryotic Glutamine Synthetase Beta-Grasp Domain' />

'''Catalytic domain'''

The catalytic domain is the C-terminal domain, extending from residues 101-382.
<applet load='Catalytic' size='300' frame='true' align='right' caption='The Prokaryotic Glutamine Synthetase Catalytic Domain' />

'''Active site'''

The dodecamer contains 12 active sites total, each formed from the Beta grasp domain of one protomer and the Catalytic domain of the neighboring protomer.
<applet load='Active_site' size='300' frame='true' align='right' caption='Insert caption here' />

{{STRUCTURE_1lgr | PDB=1lgr | SCENE= }}

User:Adrian Aldrich/Prokaryotic Glutamine Synthetase Pfam Domains Outline

2008-12-16T23:33:29Z

Adrian Aldrich:

'''Prokaryotic Glutamine Synthetase Tertiary Structure: PFam domains'''

Prokaryotic Glutamine Synthetase is a dodecamer, comprised of 12 identical polypeptide chains, organized as a dimer of two disk like hexamers. Each protomer contains 2 Pfam domains, the Beta Grasp domain and the catalytic domain, preceded by meanders of a few resides in length which link the protomers together in the dodecamers core.

'''Beta Grasp domain'''

The beta grasp domain is the N-terminal domain, extending from residues 13-94. This domain is responsible for binding ATP, Glutamate, and Ammonia. ATP binds first, activating the site for binding glutamate. <applet load='Betagrasp' size='300' frame='true' align='right' caption='The Prokaryotic Glutamine Synthetase Beta-Grasp Domain' />

'''Catalytic domain'''

The catalytic domain is the C-terminal domain, extending from residues 101-382.
<applet load='Catalytic' size='300' frame='true' align='right' caption='The Prokaryotic Glutamine Synthetase Catalytic Domain' />

'''Active site'''

The dodecamer contains 12 active sites total, each formed from the Beta grasp domain of one protomer and the Catalytic domain of the neighboring protomer.
<applet load='Active_site' size='300' frame='true' align='right' caption='Insert caption here' />

{{STRUCTURE_1lgr | PDB=1lgr | SCENE= }}

User:Adrian Aldrich/Prokaryotic Glutamine Synthetase Pfam Domains Outline

2008-12-08T01:15:30Z

Adrian Aldrich:

'''Prokaryotic Glutamine Synthetase Tertiary Structure: PFam domains'''

Prokaryotic Glutamine Synthetase is a dodecamer, comprised of 12 identical polypeptide chains, organized as a dimer of two disk like pentamers. Each protomer contains 2 Pfam domains, the Beta Grasp domain and the catalytic domain, preceded by meanders of a few resides in length which link the protomers together in the dodecamers core.

'''Beta Grasp domain'''

The beta grasp domain is the N-terminal domain, extending from residues 13-94. This domain is responsible for binding ATP, Glutamate, and Ammonia. ATP binds first, activating the site for binding glutamate. (need a more thorough description if possible.)
<show protein alignment image>
<show structures of the domain w and without ligands bound>

'''Catalytic domain'''

The catalytic domain is the C-terminal domain, extending from residues 101-382.
(mechanism is not described, more research is necessary here)

<show alignment image>
<show structures of the domain with and without ligands in viewer>

'''Active site'''

The dodecamer contains 12 active sites total, each formed from the Beta grasp domain of one protomer and the Catalytic domain of the neighboring protomer.
<show relation between chains, domains, and active sites with viewer>
-describe visually the important aspects of the active site, residues binding interactions etc..(havent generated the scenes yet)
<show active site and ligands relationship, will need multiple scenes>

Replace the PDB id after the STRUCTURE_ and after PDB= to load
and display another structure.

{{STRUCTURE_1lgr | PDB=1lgr | SCENE= }}

User:Adrian Aldrich/Prokaryotic Glutamine Synthetase Pfam Domains Outline

2008-12-08T01:14:29Z

Adrian Aldrich:

Prokaryotic Glutamine Synthetase Tertiary Structure: PFam domains

Prokaryotic Glutamine Synthetase is a dodecamer, comprised of 12 identical polypeptide chains, organized as a dimer of two disk like pentamers. Each protomer contains 2 Pfam domains, the Beta Grasp domain and the catalytic domain, preceded by meanders of a few resides in length which link the protomers together in the dodecamers core.

'''Beta Grasp domain'''
The beta grasp domain is the N-terminal domain, extending from residues 13-94. This domain is responsible for binding ATP, Glutamate, and Ammonia. ATP binds first, activating the site for binding glutamate. (need a more thorough description if possible.)
<show protein alignment image>
<show structures of the domain w and without ligands bound>

'''Catalytic domain'''
The catalytic domain is the C-terminal domain, extending from residues 101-382.
(mechanism is not described, more research is necessary here)

<show alignment image>
<show structures of the domain with and without ligands in viewer>

'''Active site'''
The dodecamer contains 12 active sites total, each formed from the Beta grasp domain of one protomer and the Catalytic domain of the neighboring protomer.
<show relation between chains, domains, and active sites with viewer>
-describe visually the important aspects of the active site, residues binding interactions etc..(havent generated the scenes yet)
<show active site and ligands relationship, will need multiple scenes>

Replace the PDB id after the STRUCTURE_ and after PDB= to load
and display another structure.

{{STRUCTURE_1lgr | PDB=1lgr | SCENE= }}

Sandbox1

2008-12-05T22:01:32Z

Adrian Aldrich:

Human Glutamine Synthetase Tertiary Structure: Pfam domains

The active site of Glutamine synthetase is the result of the interactions between two adjacent subunits.
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
-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>

Sandbox1

2008-12-05T21:25:45Z

Adrian Aldrich:

Human Glutamine Synthetase Tertiary Structure: Pfam domains

-(describe structure of protein leading in to a single chain)
-each chain contains 2 domains, 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
-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>

User:Adrian Aldrich

2008-12-05T20:06:42Z

Adrian Aldrich:

Sandbox1

2008-12-05T20:04:54Z

Adrian Aldrich:

This is just a test page.

User:Adrian Aldrich/Prokaryotic Glutamine Synthetase Pfam Domains Outline

2008-12-05T20:04:22Z

Adrian Aldrich: New page: Prokaryotic Glutamine Synthetase Tertiary Structure: PFam domains -(describe structure of protein leading in to a single chain) -each chain contains 2 domains, the Glutamine synthetase be...

Prokaryotic Glutamine Synthetase Tertiary Structure: PFam domains

-(describe structure of protein leading in to a single chain)
-each chain contains 2 domains, the Glutamine synthetase beta grasp domain, and the glutamine synthetase catalytic domain.
-the two domains are preceeded by a meander of 3-24 residues that link the chains in the proteins core.

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

Catalytic domain
-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
-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>

Replace the PDB id after the STRUCTURE_ and after PDB= to load
and display another structure.

{{STRUCTURE_3cin | PDB=3cin | SCENE= }}

User:Adrian Aldrich

2008-11-14T04:24:15Z

Adrian Aldrich:

I am a student at the University of Maryland. If you are looking for the assignment due 11/24/08 please go to...
http://www.proteopedia.org/wiki/index.php/User:Adrian_Aldrich/Section_1

User:Adrian Aldrich/Section 1

2008-11-14T04:21:37Z

Adrian Aldrich:

Here are the scenes that were created for the Scene Authoring Tools assignment. Example 4 is the scene being graded.

{{STRUCTURE_3cin | PDB=3cin | SCENE= Default }}
<scene name='User:Adrian_Aldrich/Section_1/Sec1ex1/1'>Example 1</scene>

<scene name='User:Adrian_Aldrich/Section_1/Sec1ex2/2'>Example 2</scene>

<scene name='User:Adrian_Aldrich/Section_1/Sec1ex3/1'>Example 3</scene>

<scene name='User:Adrian_Aldrich/Section_1/Sec1ex4/1'>Example 4</scene>

User:Adrian Aldrich/Section 1

2008-11-14T04:21:18Z

Adrian Aldrich:

Here are the scene that were created for the Scene Authoring Tools assignment. Example 4 is the scene being graded.

{{STRUCTURE_3cin | PDB=3cin | SCENE= Default }}
<scene name='User:Adrian_Aldrich/Section_1/Sec1ex1/1'>Example 1</scene>

<scene name='User:Adrian_Aldrich/Section_1/Sec1ex2/2'>Example 2</scene>

<scene name='User:Adrian_Aldrich/Section_1/Sec1ex3/1'>Example 3</scene>

<scene name='User:Adrian_Aldrich/Section_1/Sec1ex4/1'>Example 4</scene>

User:Adrian Aldrich/Section 1

2008-11-14T04:18:43Z

Adrian Aldrich:

test

{{STRUCTURE_3cin | PDB=3cin | SCENE= Default }}
<scene name='User:Adrian_Aldrich/Section_1/Sec1ex1/1'>Example 1</scene>

<scene name='User:Adrian_Aldrich/Section_1/Sec1ex2/2'>Example 2</scene>

<scene name='User:Adrian_Aldrich/Section_1/Sec1ex3/1'>Example 3</scene>

<scene name='User:Adrian_Aldrich/Section_1/Sec1ex4/1'>Example 4</scene>

User:Adrian Aldrich/Section 1

2008-11-14T03:53:05Z

Adrian Aldrich:

User:Adrian Aldrich/Section 1

2008-11-14T03:24:11Z

Adrian Aldrich:

test

{{STRUCTURE_3cin | PDB=3cin | SCENE=Default }}
<scene name='User:Adrian_Aldrich/Section_1/Sec1ex1/1'>Example 1</scene>

<scene name='User:Adrian_Aldrich/Section_1/Sec1ex2/2'>Example 2</scene>

User:Adrian Aldrich/Section 1

2008-11-14T03:21:03Z

Adrian Aldrich:

test

{{STRUCTURE_3cin | PDB=3cin | SCENE= }}
<scene name='User:Adrian_Aldrich/Section_1/Sec1ex1/1'>Example 1</scene>

<scene name='User:Adrian_Aldrich/Section_1/Sec1ex2/2'>Example 2</scene>

User:Adrian Aldrich/Section 1

2008-11-14T03:16:40Z

Adrian Aldrich:

test

{{STRUCTURE_3cin | PDB=3cin | SCENE= }}
<scene name='User:Adrian_Aldrich/Section_1/Sec1ex1/1'>Example 1</scene>

<scene name='User:Adrian_Aldrich/Section_1/Sec1ex2/1'>Example 2</scene>

User:Adrian Aldrich/Section 1

2008-11-14T02:55:32Z

Adrian Aldrich:

test

{{STRUCTURE_3cin | PDB=3cin | SCENE= }}
<scene name='User:Adrian_Aldrich/Section_1/Sec1ex1/1'>Example 1</scene>

User:Adrian Aldrich/Section 1

2008-11-14T02:53:12Z

Adrian Aldrich:

test

<scene name='User:Adrian_Aldrich/Section_1/Sec1ex1/1'>Example 1</scene>

User:Adrian Aldrich/Section 1

2008-11-14T02:51:25Z

Adrian Aldrich:

test

<scene name='User:Adrian_Aldrich/Section_1/Sec1ex1/1'>TextToBeDisplayed</scene>

User:Adrian Aldrich/Section 1

2008-11-14T02:38:56Z

Adrian Aldrich: New page: ==This is a placeholder== This is a placeholder text to help you get started in placing a Jmol applet on your page. At any time, click "Show Preview" at the bottom of this page to see how...

==This is a placeholder==
This is a placeholder text to help you get started in
placing a Jmol applet on your page. At any time, click
"Show Preview" at the bottom of this page to see how it goes.

Replace the PDB id after the STRUCTURE_ and after PDB= to load
and display another structure.

{{STRUCTURE_3cin | PDB=3cin | SCENE= }}

test