Glutamate synthase: Difference between revisions

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<StructureSection load='1llw' size='340' side='right' caption='Ferredoxin-dependent glutamate synthase containing a Fe3S4 cluster complex with FMN, 2-oxoglutarate (PDB code [[1llw]])' scene=''>
<StructureSection load='' size='350' side='right' caption='Ferredoxin-dependent glutamate synthase containing a Fe3S4 cluster complex with FMN, 2-oxoglutarate (PDB code [[1llw]])' scene='72/727110/Cv/1'>
== Function ==
== Function ==
'''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.
'''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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== 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>.
The <scene name='72/727110/Cv/10'>Fd-GS structure contains 4 domains</scene>.  The N-terminal domain is an amidotransferase domain and contains an active site where <scene name='72/727110/Cv/11'>residue Cys1</scene> catalyzes the hydrolysis of glutamine to glutarate; a core domain; an FMN-binding domain which <scene name='72/727110/Cv/12'>contains an Fe3S4 cluster</scene> and reduces the intermediate iminoglutarate to 2-oxoglutarate and produces a second molecule of glutarate and a C-terminal domain.  <scene name='72/727110/Cv/13'>Residue M475 is located between the FMN and the Fe3S4 cluster</scene>. It is is strictly conserved and may perform the electron transfer between the two centers. <scene name='72/727110/Cv/14'>FMN binding site</scene> The <scene name='72/727110/Cv/15'>2-oxoglutarate binds at the FMN-binding domain</scene><ref>PMID:11967268</ref>.


</StructureSection>
</StructureSection>
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**[[1ea0]] – AbGS α subunit + FMN + oxo-glutarate – ''Azospirillum brasilense''<br />
**[[1ea0]] – AbGS α subunit + FMN + oxo-glutarate – ''Azospirillum brasilense''<br />
**[[2vdc]] – AbGS α+β subunits + FAD + FMN + oxoglutarate – CryoEM<br />
**[[6s6s]], [[6s6t]], [[6s6u]], [[6s6x]] – AbGS α+β subunits + FAD + FMN + Fe3S4 + Fe4S4 – CryoEM<br />
**[[2vdc]] – AbGS α+β subunits + FAD + FMN + Fe3S4 + Fe4S4 + oxoglutarate – CryoEM<br />
**[[7mfm]], [[7mft]] – GS + glutamate dehydrogenase – ''Bacillus subtilis'' - CryoEM<br />


*Fd-dependent glutamate synthase
*Fd-dependent glutamate synthase
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== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]

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Michal Harel, Alexander Berchansky, Joel L. Sussman