Sandbox2qc8
From Proteopedia
(Difference between revisions)
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- | Each subunit has an exposed NH2 terminus and buried COOH terminus as part of a <scene name='Sandbox2qc8/Ntocterminuswiththong/1'>helical thong</scene>. <ref>Yamashita, M., et al.,Refined Atomic Model of Glutamine Synthetase at 3.5A Resolution, The Journal of Biological Chemistry, 1989, 17681-17690.</ref> | + | Each subunit has an exposed NH2 terminus and buried COOH terminus as part of a <scene name='Sandbox2qc8/Ntocterminuswiththong/1'>helical thong</scene>, colored in red. The helical thong is used as an anchor inside another subunit. <ref>Yamashita, M., et al.,Refined Atomic Model of Glutamine Synthetase at 3.5A Resolution, The Journal of Biological Chemistry, 1989, 17681-17690.</ref> |
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The only ligand present is a pair of Mn ions (Manganese) that indicates the active site of each subunit of the dodecamer. | The only ligand present is a pair of Mn ions (Manganese) that indicates the active site of each subunit of the dodecamer. | ||
- | <scene name='Sandbox2qc8/Catalytic_sites/1'> | + | Glutamine synthetase contains the <scene name='Sandbox2qc8/Catalytic_sites/1'>catalytic sites E327, R339, D50</scene>.<br> |
Revision as of 18:36, 19 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 , colored in red. The helical thong is used as an anchor inside another subunit. [1]
The beta strands are arranged into five . In addition, there are 5 and 5 . [2]
The active site within the secondary structure can be called a "bifunnel," providing access to ATP and glutamate at opposing ends.[3]
The only ligand present is a pair of Mn ions (Manganese) that indicates the active site of each subunit of the dodecamer.
Glutamine synthetase contains the .
References
- ↑ Yamashita, M., et al.,Refined Atomic Model of Glutamine Synthetase at 3.5A Resolution, The Journal of Biological Chemistry, 1989, 17681-17690.
- ↑ European Bioinformatics Institute, Ligase(amide synthetase), http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=2gls, Accessed December 18, 2008.
- ↑ Eisenberg, D., et al., Structure-function relationships of glutamine synthetases, Biochimica et Biophysica Acta 1477 (2000), 122-145.