User talk:Adrian Aldrich/Prokaryotic Glutamine Synthetase Pfam Domains
From Proteopedia
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'''Prokaryotic Glutamine Synthetase Tertiary Structure: PFam domains''' | '''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. | + | 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''' | '''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. | + | 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''' | '''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. | + | 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]. |
Current revision
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| 1lgr, resolution 2.79Å () | |||||||||
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| Ligands: | , | ||||||||
| Activity: | Glutamate--ammonia ligase, with EC number 6.3.1.2 | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Prokaryotic Glutamine Synthetase Tertiary Structure: PFam domains
Prokaryotic Glutamine Synthetase[1] is a dodecamer, comprised of 12 identical polypeptide chains, organized as a dimer of two disk like hexamers. Each protomer contains 2 Pfam[2] 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[3], Glutamate[4], and Ammonia[5]. The domain folds into a bent beta-sheet[6] flanked by two short alpha helices[7], forming a pocket for the ligands to bind. ATP[8] 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[9] coated on one side by several alpha helices[10].
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.
