Sandbox2qc8

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Glutamine synthetase is composed of 10 <scene name='Sandbox2qc8/Secondary_structure/1'>identical subunits</scene>.
Glutamine synthetase is composed of 10 <scene name='Sandbox2qc8/Secondary_structure/1'>identical subunits</scene>.
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Each subunit has an exposed NH2 terminus and buried COOH terminus. <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 is composed predominantly of 12 <scene name='Sandbox2qc8/Subunit_alpha/1'>alpha helices</scene> and 12
Each subunit is composed predominantly of 12 <scene name='Sandbox2qc8/Subunit_alpha/1'>alpha helices</scene> and 12
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The beta sheets are arranged into two separate partial beta barrels, one of which encompasses the ligand complex.
The beta sheets are arranged into two separate partial beta barrels, one of which encompasses the ligand complex.
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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> <br/> <br/>
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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>

Revision as of 02:59, 8 December 2008

PDB ID 2qc8

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2qc8, resolution 2.60Å ()
Ligands: , , ,
Gene: GLUL, GLNS (Homo sapiens)
Activity: Glutamate--ammonia ligase, with EC number 6.3.1.2
Related: 2ojw
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



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Glutamine synthetase is composed of 10 .

Each subunit has an exposed NH2 terminus and buried COOH terminus. [1]

Each subunit is composed predominantly of 12 and 12 , as well as a .

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 ligands present are Cl, Mn, Adenosine Diphosphate, and L-Methionine-S-Sulfoximine Phosphate.

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.
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