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{{STRUCTURE_2ojw| PDB=2ojw | SCENE= }} | {{STRUCTURE_2ojw| PDB=2ojw | SCENE= }} | ||
===Crystal structure of human glutamine synthetase in complex with ADP and phosphate=== | |||
{{ABSTRACT_PUBMED_18005987}} | |||
=== | ==Disease== | ||
[[http://www.uniprot.org/uniprot/GLNA_HUMAN GLNA_HUMAN]] Defects in GLUL are the cause of congenital systemic glutamine deficiency (CSGD) [MIM:[http://omim.org/entry/610015 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.<ref>PMID:16267323</ref> | |||
==Function== | |||
[[http://www.uniprot.org/uniprot/GLNA_HUMAN 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.<ref>PMID:18662667</ref> | |||
==About this Structure== | ==About this Structure== | ||
| Line 14: | Line 16: | ||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID:018005987</ref><references group="xtra"/> | <ref group="xtra">PMID:018005987</ref><references group="xtra"/><references/> | ||
[[Category: Glutamate--ammonia ligase]] | [[Category: Glutamate--ammonia ligase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
Revision as of 14:46, 24 March 2013
Crystal structure of human glutamine synthetase in complex with ADP and phosphateCrystal structure of human glutamine synthetase in complex with ADP and phosphate
Template:ABSTRACT PUBMED 18005987
DiseaseDisease
[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]
FunctionFunction
[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 StructureAbout this Structure
2ojw is a 5 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See AlsoSee Also
ReferenceReference
- ↑ 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
- ↑ 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
- ↑ 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
Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCACategories:
- Glutamate--ammonia ligase
- Homo sapiens
- Arrowsmith, C.
- Berg, S Van Den.
- Berglund, H.
- Busam, R D.
- Collins, R.
- Edwards, A.
- Flodin, S.
- Flores, A.
- Graslund, S.
- Hallberg, B M.
- Hammarstrom, M.
- Hogbom, M.
- Holmberg-Schiavone, L.
- Johansson, I.
- Karlberg, T.
- Kotenyova, T.
- Moche, M.
- Nilsson, M E.
- Nordlund, P.
- Nyman, T.
- Ogg, D.
- Persson, C.
- SGC, Structural Genomics Consortium.
- Sagemark, J.
- Stenmark, P.
- Sundstrom, M.
- Thorsell, A G.
- Uppenberg, J.
- Wallden, K.
- Weigelt, J.
- Amino-acid biosynthesis
- Ligase
- Sgc
- Structural genomic
- Structural genomics consortium
- Synthetase