2qc8

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spinqualitylabelsall models PDB ID 2qc8 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
2qc8, resolution 2.60Å ()
Ligands:	, , ,
Gene:	GLUL, GLNS (Homo sapiens)
Activity:	Glutamate--ammonia ligase, with EC number 6.3.1.2
Related:	2ojw
Structural annotation: Resources: InterPro : Ipr014746, Ipr008147, Ipr008146 Pfam : PF00120, PF03951 UniProt : P15104
Functional annotation: Cellular component: cytoplasm Biological process: nitrogen compound metabolic process glutamine biosynthetic process regulation of neurotransmitter levels Molecular function: ligase activity 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, RCSB, PDBsum
Coordinates:	save as pdb, mmCIF, xml

Contents 1 Crystal structure of human glutamine synthetase in complex with ADP and methionine sulfoximine phosphate 2 Disease 3 Function 4 About this Structure 5 See Also 6 Reference

Crystal structure of human glutamine synthetase in complex with ADP and methionine sulfoximine phosphate

Template:ABSTRACT PUBMED 18005987

Disease

[GLNA_HUMAN] Defects in GLUL are the cause of congenital systemic glutamine deficiency (CSGD) [MIM:610015]. CSGD is a rare developmental disorder with severe brain malformation resulting in multi-organ failure and neonatal death. Glutamine is largely absent from affected patients serum, urine and cerebrospinal fluid.^[1]

Function

[GLNA_HUMAN] This enzyme has 2 functions: it catalyzes the production of glutamine and 4-aminobutanoate (gamma-aminobutyric acid, GABA), the latter in a pyridoxal phosphate-independent manner (By similarity). Essential for proliferation of fetal skin fibroblasts.^[2]

About this Structure

2qc8 is a 10 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

See Also

• Glutamine Synthase

Reference

• Krajewski WW, Collins R, Holmberg-Schiavone L, Jones TA, Karlberg T, Mowbray SL. Crystal structures of mammalian glutamine synthetases illustrate substrate-induced conformational changes and provide opportunities for drug and herbicide design. J Mol Biol. 2008 Jan 4;375(1):217-28. Epub 2007 Oct 17. PMID:18005987 doi:10.1016/j.jmb.2007.10.029

1. ↑ Haberle J, Gorg B, Rutsch F, Schmidt E, Toutain A, Benoist JF, Gelot A, Suc AL, Hohne W, Schliess F, Haussinger D, Koch HG. Congenital glutamine deficiency with glutamine synthetase mutations. N Engl J Med. 2005 Nov 3;353(18):1926-33. PMID:16267323 doi:353/18/1926
2. ↑ Vermeulen T, Gorg B, Vogl T, Wolf M, Varga G, Toutain A, Paul R, Schliess F, Haussinger D, Haberle J. Glutamine synthetase is essential for proliferation of fetal skin fibroblasts. Arch Biochem Biophys. 2008 Oct 1;478(1):96-102. doi: 10.1016/j.abb.2008.07.009., Epub 2008 Jul 17. PMID:18662667 doi:10.1016/j.abb.2008.07.009