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Revision as of 22:26, 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.
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.
