User:Adrian Aldrich/Prokaryotic Glutamine Synthetase Pfam Domains Outline

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'''Prokaryotic Glutamine Synthetase Tertiary Structure: PFam domains'''
'''Prokaryotic Glutamine Synthetase Tertiary Structure: PFam domains'''
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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.
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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'''
'''Beta Grasp domain'''
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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.)
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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' />
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<show protein alignment image>
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<show structures of the domain w and without ligands bound>
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'''Catalytic domain'''
'''Catalytic domain'''
The catalytic domain is the C-terminal domain, extending from residues 101-382.
The catalytic domain is the C-terminal domain, extending from residues 101-382.
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(mechanism is not described, more research is necessary here)
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<applet load='Catalytic' size='300' frame='true' align='right' caption='The Prokaryotic Glutamine Synthetase Catalytic Domain' />
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<show alignment image>
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<show structures of the domain with and without ligands in viewer>
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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.
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.
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<show relation between chains, domains, and active sites with viewer>
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<applet load='Active_site' size='300' frame='true' align='right' caption='Insert caption here' />
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-describe visually the important aspects of the active site, residues binding interactions etc..(havent generated the scenes yet)
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<show active site and ligands relationship, will need multiple scenes>
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Replace the PDB id after the STRUCTURE_ and after PDB= to load
 
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and display another structure.
 
{{STRUCTURE_1lgr | PDB=1lgr | SCENE= }}
{{STRUCTURE_1lgr | PDB=1lgr | SCENE= }}

Revision as of 23:33, 16 December 2008

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.

The Prokaryotic Glutamine Synthetase Beta-Grasp Domain

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Catalytic domain

The catalytic domain is the C-terminal domain, extending from residues 101-382.

The Prokaryotic Glutamine Synthetase Catalytic Domain

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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.

Insert caption here

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PDB ID 1lgr

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1lgr, resolution 2.79Å ()
Ligands: ,
Activity: Glutamate--ammonia ligase, with EC number 6.3.1.2
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml


Proteopedia Page Contributors and Editors (what is this?)

Adrian Aldrich

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