Sandbox2qc8

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(→Glutamine Synthetase: Secondary structures)
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Each subunit has an exposed NH2 terminus and buried COOH terminus as part of a helical thong. <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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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>
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The beta sheets are arranged into two separate partial beta barrels, one of which encompasses the ligand complex.
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The beta strands are arranged into five <scene name='Sandbox2qc8/Pdb_defined_beta_strands/1'>beta sheets</scene>.
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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>
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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.
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<scene name='Sandbox2qc8/Pdb_defined_beta_strands/1'>New strands.</scene>,
 
<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'>Catalytic sites E327, R339, D50</scene><br>
<scene name='Sandbox2qc8/Catalytic_sites/1'>Catalytic sites E327, R339, D50</scene><br>
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<scene name='Sandbox2qc8/Ntocterminuswiththong/1'>N to C terminus embedding and thong in red</scene>
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=References=
=References=
<references/>
<references/>
[[Image:Example.jpg]]
[[Image:Example.jpg]]

Revision as of 23:52, 18 December 2008

PDB ID 2gls

Drag the structure with the mouse to rotate
2gls, resolution 3.50Å ()
Ligands:
Activity: Glutamate--ammonia ligase, with EC number 6.3.1.2
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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 . [1]


The beta strands are arranged into five . .

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

  1. ↑ Yamashita, M., et al.,Refined Atomic Model of Glutamine Synthetase at 3.5A Resolution, The Journal of Biological Chemistry, 1989, 17681-17690.
  2. ↑ Eisenberg, D., et al., Structure-function relationships of glutamine synthetases, Biochimica et Biophysica Acta 1477 (2000), 122-145.

Image:Example.jpg

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