Glutamate synthase

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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 ==
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'''Glutamate synthase''' (GS) catalyzes the reverse reaction which converts L-glutamine, 2-oxo-glutarate and NADPH to L-glutarate and NADP.
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'''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.
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<ref>PMID:18421771</ref>. Fd-dependent glutamate synthase catalyzes the reverse reaction converting L-glutamate and oxidized ferredoxin to L-glutamine, 2-oxo-glutarate and oxidized ferredoxin<ref>PMID:6746604</ref>.
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<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 ==
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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
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**[[1ea0]] – AbGS alpha subunit + FMN + oxo-glutarate – ''Azospirillum brasilense''<br />
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**[[1ea0]] – AbGS α subunit + FMN + oxo-glutarate – ''Azospirillum brasilense''<br />
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**[[2vdc]] – AbGS alpha+beta subunits + FAD + FMN + oxo-glutarate – CryoEM<br />
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**[[2vdc]] – AbGS α+β subunits + FAD + FMN + oxoglutarate – CryoEM<br />
*Fd-dependent glutamate synthase
*Fd-dependent glutamate synthase
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**[[1llw]], [[1ofd]] – SyGS + FMN + oxo-glutarate – ''Synechocystis''<br />
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**[[1llw]], [[1ofd]] – SyGS + FMN + 2-αoxoglutarate – ''Synechocystis''<br />
**[[1llz]], [[1lm1]] – SyGS + FMN <br />
**[[1llz]], [[1lm1]] – SyGS + FMN <br />
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**[[1ofe]] – SyGS + FMN + oxglutarate + oxo-norleucine<br />
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**[[1ofe]] – SyGS + FMN + 2-oxglutarate + oxo-norleucine<br />
}}
}}
== References ==
== References ==
<references/>
<references/>

Revision as of 09:50, 9 March 2016

Ferredoxin-dependent glutamate synthase containing a Fe3-S4 cluster complex with FMN, 2-oxo-glutarate (PDB code 1llw)

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3D structures of glutamate synthase

Updated on 09-March-2016

References

  1. 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
  2. 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
  3. 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

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