Sandbox2qc8

(Difference between revisions)

Revision as of 17:44, 17 December 2008

Ligands:

Activity:

Glutamate--ammonia ligase, with EC number 6.3.1.2

Structural annotation:

Resources:

Functional annotation:
Cellular component:	cytoplasm
Biological process:	nitrogen compound metabolic process glutamine biosynthetic process nitrogen fixation
Molecular function:	ligase activity nucleotide binding glutamate-ammonia ligase activity catalytic activity

Evolutionary conservation:

Toggle Conservation Colors:	Rows = identical sequences:
Further Information:	Caveats, Explanation, Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, PDBsum, RCSB

Coordinates:

save as pdb, mmCIF, xml

Glutamine synthetase is composed of 12 . Each subunit is composed of 15 and 12 , as well as a .

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

↑ 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.

@@ Line 4: / Line 4: @@
 Glutamine synthetase is composed of 12 <scene name='Sandbox2qc8/Identical_subunits/1'>identical subunits</scene>. Each subunit is composed of 15 <scene name='Sandbox2qc8/15_alpha_helices/1'>alpha helices</scene> and 12
-<scene name='Sandbox2qc8/Subunit_beta/1'>beta sheets</scene>, as well as a <scene name='Sandbox2qc8/Subunit_ligand/1'>ligand complex</scene>.
+<scene name='Sandbox2qc8/Beta_sheets/1'>beta sheets</scene>, as well as a <scene name='Sandbox2qc8/Subunit_ligand/1'>ligand complex</scene>.
 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>