This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
Sandbox2qc8
From Proteopedia
Glutamine Synthetase: Secondary structures
Glutamine synthetase is composed of 12 . Each subunit is composed of 15 and 15 . 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.
