Sandbox2qc8
From Proteopedia
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<scene name='Sandbox2qc8/Hairpins/1'>Hairpins</scene>, | <scene name='Sandbox2qc8/Hairpins/1'>Hairpins</scene>, | ||
<scene name='Sandbox2qc8/Bulges/1'>Bulges</scene>, | <scene name='Sandbox2qc8/Bulges/1'>Bulges</scene>, | ||
| - | <scene name='Sandbox2qc8/Catalytic_sites/1'> | + | <scene name='Sandbox2qc8/Catalytic_sites/1'>Catalytic sites E327, R339, D50</scene><br> |
<scene name='Sandbox2qc8/Ntocterminuswiththong/1'>N to C terminus embedding and thong in red</scene> | <scene name='Sandbox2qc8/Ntocterminuswiththong/1'>N to C terminus embedding and thong in red</scene> | ||
Revision as of 23:18, 18 December 2008
Glutamine Synthetase: Secondary structures
Glutamine synthetase is composed of 12 . Each subunit is composed of 15 and . Each subunit binds 2 Mn for a total of per Glutamine Synthetase.
Each subunit has an exposed NH2 terminus and buried COOH terminus as part of a helical thong. [1]
The beta sheets are arranged into two separate partial beta barrels, one of which encompasses the ligand complex.
The active site within the secondary structure can be called a "bifunnel," providing access to ATP and glutamate at opposing ends.[2]
The only ligand present is a pair of Mn ions (Manganese) that indicates the active site of each subunit of the dodecamer.
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References
- ↑ Yamashita, M., et al.,Refined Atomic Model of Glutamine Synthetase at 3.5A Resolution, The Journal of Biological Chemistry, 1989, 17681-17690.
- ↑ Eisenberg, D., et al., Structure-function relationships of glutamine synthetases, Biochimica et Biophysica Acta 1477 (2000), 122-145.
