User:Adrian Aldrich/Prokaryotic Glutamine Synthetase Pfam Domains Outline
From Proteopedia
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| + | {{STRUCTURE_1lgr | PDB=1lgr | SCENE= }} | ||
'''Prokaryotic Glutamine Synthetase Tertiary Structure: PFam domains''' | '''Prokaryotic Glutamine Synthetase Tertiary Structure: PFam domains''' | ||
| - | {{STRUCTURE_1lgr | PDB=1lgr | SCENE= }} | ||
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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 | + | 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''' | '''Beta Grasp domain''' | ||
| - | The | + | 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> | <scene name='User:Adrian_Aldrich/Prokaryotic_Glutamine_Synthetase_Pfam_Domains_Outline/Betagrasp/1'>Prokaryotic Glutamine Synthetase Beta-Grasp Domain</scene> | ||
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'''Active site''' | '''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. | + | 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> | <scene name='User:Adrian_Aldrich/Prokaryotic_Glutamine_Synthetase_Pfam_Domains_Outline/Active_site/1'>Prokaryotic Glutamine Synthetase Active site</scene> | ||
Revision as of 00:22, 17 December 2008
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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 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.
Catalytic domain
The catalytic domain is the C-terminal domain, extending from residues 101-382.
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.
