1ofd: Difference between revisions
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'''GLUTAMATE SYNTHASE FROM SYNECHOCYSTIS SP IN COMPLEX WITH 2-OXOGLUTARATE AT 2.0 ANGSTROM RESOLUTION''' | '''GLUTAMATE SYNTHASE FROM SYNECHOCYSTIS SP IN COMPLEX WITH 2-OXOGLUTARATE AT 2.0 ANGSTROM RESOLUTION''' | ||
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==Reference== | ==Reference== | ||
The active conformation of glutamate synthase and its binding to ferredoxin., van den Heuvel RH, Svergun DI, Petoukhov MV, Coda A, Curti B, Ravasio S, Vanoni MA, Mattevi A, J Mol Biol. 2003 Jun 27;330(1):113-28. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12818206 12818206] | The active conformation of glutamate synthase and its binding to ferredoxin., van den Heuvel RH, Svergun DI, Petoukhov MV, Coda A, Curti B, Ravasio S, Vanoni MA, Mattevi A, J Mol Biol. 2003 Jun 27;330(1):113-28. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12818206 12818206] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Synechocystis sp.]] | [[Category: Synechocystis sp.]] | ||
[[Category: Heuvel, R H.H Van Den.]] | [[Category: Heuvel, R H.H Van Den.]] | ||
[[Category: Mattevi, A.]] | [[Category: Mattevi, A.]] | ||
[[Category: | [[Category: Amidotransferase]] | ||
[[Category: | [[Category: Complex enzyme]] | ||
[[Category: | [[Category: Fad]] | ||
[[Category: | [[Category: Fd-gogat]] | ||
[[Category: | [[Category: Flavoprotein]] | ||
[[Category: | [[Category: Fmn]] | ||
[[Category: | [[Category: Iron-sulphur]] | ||
[[Category: | [[Category: Oxidoreductase]] | ||
[[Category: | [[Category: Substrate channeling]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:46:42 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 03:46, 3 May 2008
GLUTAMATE SYNTHASE FROM SYNECHOCYSTIS SP IN COMPLEX WITH 2-OXOGLUTARATE AT 2.0 ANGSTROM RESOLUTION
OverviewOverview
Glutamate synthases (GltS) are crucial enzymes in ammonia assimilation in plants and bacteria, where they catalyze the formation of two molecules of L-glutamate from L-glutamine and 2-oxoglutarate. The plant-type ferredoxin-dependent GltS and the functionally homologous alpha subunit of the bacterial NADPH-dependent GltS are complex four-domain monomeric enzymes of 140-165 kDa belonging to the NH(2)-terminal nucleophile family of amidotransferases. The enzymes function through the channeling of ammonia from the N-terminal amidotransferase domain to the FMN-binding domain. Here, we report the X-ray structure of the Synechocystis ferredoxin-dependent GltS with the substrate 2-oxoglutarate and the covalent inhibitor 5-oxo-L-norleucine bound in their physically distinct active sites solved using a new crystal form. The covalent Cys1-5-oxo-L-norleucine adduct mimics the glutamyl-thioester intermediate formed during L-glutamine hydrolysis. Moreover, we determined a high resolution structure of the GltS:2-oxoglutarate complex. These structures represent the enzyme in the active conformation. By comparing these structures with that of GltS alpha subunit and of related enzymes we propose a mechanism for enzyme self-regulation and ammonia channeling between the active sites. X-ray small-angle scattering experiments were performed on solutions containing GltS and its physiological electron donor ferredoxin (Fd). Using the structure of GltS and the newly determined crystal structure of Synechocystis Fd, the scattering experiments clearly showed that GltS forms an equimolar (1:1) complex with Fd. A fundamental consequence of this result is that two Fd molecules bind consecutively to Fd-GltS to yield the reduced FMN cofactor during catalysis.
About this StructureAbout this Structure
1OFD is a Single protein structure of sequence from Synechocystis sp.. Full crystallographic information is available from OCA.
ReferenceReference
The active conformation of glutamate synthase and its binding to ferredoxin., van den Heuvel RH, Svergun DI, Petoukhov MV, Coda A, Curti B, Ravasio S, Vanoni MA, Mattevi A, J Mol Biol. 2003 Jun 27;330(1):113-28. PMID:12818206 Page seeded by OCA on Sat May 3 03:46:42 2008