Glutamine synthetase

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=Structure=
=Structure=
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An unrefined structure of glutamine synthetase is made of two layers, each containing 6 subunits, for a total of 12 subunits. <ref>PMID:2572586 </ref> Each active site is defined by a cylindrical shape formed by six antiparalel β starnds contributed by one subunit and two strands by the neighbouring subunit.<ref>PMID:2572586 </ref>
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An unrefined structure of glutamine synthetase is made of two layers, each containing 6 subunits, for a total of 12 subunits. <ref>PMID:2572586 </ref> Each active site is defined by a cylindrical shape formed by six antiparalel β starnds contributed by one subunit and two strands by the neighbouring subunit.<ref>PMID:2572586 </ref> In each cylindrical active site there are two Mn2+ ions, both of which are have three protein chains and two water molecules, one water shared by both Mn2+. For the protein ligands to Mn 2+ 469, Glu-131, GLu-212 and Glu-220 are attached and for the Mn2+, Glu-129, His-269 and Glu-357 are designated.
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[[Image:Example.jpg]]
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Revision as of 06:51, 24 March 2010

Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. Andrea Gorrell.

Contents

Rhiannon Khela

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



Structure

An unrefined structure of glutamine synthetase is made of two layers, each containing 6 subunits, for a total of 12 subunits. [1] Each active site is defined by a cylindrical shape formed by six antiparalel β starnds contributed by one subunit and two strands by the neighbouring subunit.[2] In each cylindrical active site there are two Mn2+ ions, both of which are have three protein chains and two water molecules, one water shared by both Mn2+. For the protein ligands to Mn 2+ 469, Glu-131, GLu-212 and Glu-220 are attached and for the Mn2+, Glu-129, His-269 and Glu-357 are designated.


Function

Glutamine synthetase is an essential enzyme in the cellular nitrogen metabolism and has been found to play a role in both ammonia assimilation and glutamine byosynthesis.[3] Image:Glutamine-synthesis.jpg

References

  1. ↑ Yamashita MM, Almassy RJ, Janson CA, Cascio D, Eisenberg D. Refined atomic model of glutamine synthetase at 3.5 A resolution. J Biol Chem. 1989 Oct 25;264(30):17681-90. PMID:2572586
  2. ↑ Yamashita MM, Almassy RJ, Janson CA, Cascio D, Eisenberg D. Refined atomic model of glutamine synthetase at 3.5 A resolution. J Biol Chem. 1989 Oct 25;264(30):17681-90. PMID:2572586
  3. ↑ Kumada Y, Benson DR, Hillemann D, Hosted TJ, Rochefort DA, Thompson CJ, Wohlleben W, Tateno Y. Evolution of the glutamine synthetase gene, one of the oldest existing and functioning genes. Proc Natl Acad Sci U S A. 1993 Apr 1;90(7):3009-13. PMID:8096645


Image:2gls120.png
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