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The active site within the secondary structure can be called a "bifunnel," providing access to ATP and glutamate at opposing ends.<ref>Eisenberg, D., et al., Structure-function relationships of glutamine synthetases, Biochimica et Biophysica Acta 1477 (2000), 122-145.</ref> | The active site within the secondary structure can be called a "bifunnel," providing access to ATP and glutamate at opposing ends.<ref>Eisenberg, D., et al., Structure-function relationships of glutamine synthetases, Biochimica et Biophysica Acta 1477 (2000), 122-145.</ref> | ||
| - | The only ligand present is a pair of Mn ions (Manganese) that the active site of each subunit. | + | The only ligand present is a pair of Mn ions (Manganese) that indicates the active site of each subunit of the dodecamer. |
=References= | =References= | ||
<references/> | <references/> | ||
[[Image:Example.jpg]] | [[Image:Example.jpg]] | ||
Revision as of 05:01, 18 December 2008
Glutamine Synthetase: Secondary structures
Glutamine synthetase is composed of 12 . Each subunit is composed of 15 and 12 , as well as a .
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.
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.
