User:Adrian Aldrich/Prokaryotic Glutamine Synthetase Pfam Domains Outline

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{{STRUCTURE_1lgr | PDB=1lgr | SCENE= }}
'''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 at the N terminus by short chains(3-13)of resides which link the all protomers together in the dodecamers core.
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'''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 <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.
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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'''
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The catalytic domain is the C-terminal domain, extending from residues 101-382.
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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.
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(mechanism is not described, more research is necessary here)
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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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'''Active site'''
'''Active site'''
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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.
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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.
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<show relation between chains, domains, and active sites with viewer>
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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.
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{{STRUCTURE_1lgr | PDB=1lgr | SCENE= }}
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Current revision

PDB ID 1lgr

Drag the structure with the mouse to rotate
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


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 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 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 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.

Proteopedia Page Contributors and Editors (what is this?)

Adrian Aldrich

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