Glutamate synthase
From Proteopedia
(Difference between revisions)
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<StructureSection load='1llw' size='340' side='right' caption='Ferredoxin-dependent glutamate synthase containing a Fe3-S4 cluster complex with FMN, 2-oxo-glutarate (PDB code [[1llw]])' scene=''> | <StructureSection load='1llw' size='340' side='right' caption='Ferredoxin-dependent glutamate synthase containing a Fe3-S4 cluster complex with FMN, 2-oxo-glutarate (PDB code [[1llw]])' scene=''> | ||
== Function == | == Function == | ||
- | '''Glutamate synthase''' (GS) catalyzes the reverse reaction which converts L-glutamine, 2- | + | '''Glutamate synthase''' (GS) is an iron-sulfur flavoprotein which catalyzes the reverse reaction which converts L-glutamine, 2-oxoglutarate and NADPH to L-glutarate and NADP. |
- | <ref>PMID:18421771</ref>. Fd-dependent glutamate synthase catalyzes the reverse reaction converting L-glutamate and oxidized ferredoxin to L-glutamine, 2- | + | <ref>PMID:18421771</ref>. Fd-dependent glutamate synthase catalyzes the reverse reaction converting L-glutamate and oxidized ferredoxin to L-glutamine, 2-oxoglutarate and oxidized ferredoxin<ref>PMID:6746604</ref>. Fd-GS uses FMN as a cofactor. |
== Disease == | == Disease == | ||
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== Structural highlights == | == Structural highlights == | ||
- | + | The Fd-GS structure contains 4 domains. The N-terminal domain is an amidotransferase domain and contains an active site where residue 1Cys catalyzes the hydrolysis of glutamine to glutarate; a core domain; an FMN-binding domain which contains an Fe3S4 cluster and reduces the intermediate iminoglutarate to 2-oxoglutarate and produces a second molecule of glutarate and a C-terminal domain. Residue M475 is located between the FMN and the Fe3S4 cluster. It is is strictly conserved and may perform the electron transfer between the two centers. The 2-oxoglutarate binds at the FMN-binding domain<ref>PMID:11967268</ref>. | |
</StructureSection> | </StructureSection> | ||
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*Glutamate synthase | *Glutamate synthase | ||
- | **[[1ea0]] – AbGS | + | **[[1ea0]] – AbGS α subunit + FMN + oxo-glutarate – ''Azospirillum brasilense''<br /> |
- | **[[2vdc]] – AbGS | + | **[[2vdc]] – AbGS α+β subunits + FAD + FMN + oxoglutarate – CryoEM<br /> |
*Fd-dependent glutamate synthase | *Fd-dependent glutamate synthase | ||
- | **[[1llw]], [[1ofd]] – SyGS + FMN + | + | **[[1llw]], [[1ofd]] – SyGS + FMN + 2-αoxoglutarate – ''Synechocystis''<br /> |
**[[1llz]], [[1lm1]] – SyGS + FMN <br /> | **[[1llz]], [[1lm1]] – SyGS + FMN <br /> | ||
- | **[[1ofe]] – SyGS + FMN + oxglutarate + oxo-norleucine<br /> | + | **[[1ofe]] – SyGS + FMN + 2-oxglutarate + oxo-norleucine<br /> |
}} | }} | ||
== References == | == References == | ||
<references/> | <references/> |
Revision as of 09:50, 9 March 2016
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3D structures of glutamate synthase
Updated on 09-March-2016
References
- ↑ Vanoni MA, Curti B. Structure-function studies of glutamate synthases: a class of self-regulated iron-sulfur flavoenzymes essential for nitrogen assimilation. IUBMB Life. 2008 May;60(5):287-300. doi: 10.1002/iub.52. PMID:18421771 doi:http://dx.doi.org/10.1002/iub.52
- ↑ Hirasawa M, Tamura G. Flavin and iron-sulfur containing ferredoxin-linked glutamate synthase from spinach leaves. J Biochem. 1984 Apr;95(4):983-94. PMID:6746604
- ↑ van den Heuvel RH, Ferrari D, Bossi RT, Ravasio S, Curti B, Vanoni MA, Florencio FJ, Mattevi A. Structural studies on the synchronization of catalytic centers in glutamate synthase. J Biol Chem. 2002 Jul 5;277(27):24579-83. Epub 2002 Apr 19. PMID:11967268 doi:10.1074/jbc.M202541200