1ofd: Difference between revisions
New page: left|200px<br /> <applet load="1ofd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ofd, resolution 2.0Å" /> '''GLUTAMATE SYNTHASE F... |
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==About this Structure== | ==About this Structure== | ||
1OFD is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Synechocystis_sp. Synechocystis sp.]] with FMN, F3S and AKG as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.7.1 1.4.7.1]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OFD OCA]]. | 1OFD is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Synechocystis_sp. Synechocystis sp.]] with FMN, F3S and AKG as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Glutamate_synthase_(ferredoxin) Glutamate synthase (ferredoxin)]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.7.1 1.4.7.1]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OFD OCA]]. | ||
==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://ispc.weizmann.ac.il//pmbin/getpm?pmid=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://ispc.weizmann.ac.il//pmbin/getpm?pmid=12818206 12818206] | ||
[[Category: Glutamate synthase (ferredoxin)]] | |||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Synechocystis sp.]] | [[Category: Synechocystis sp.]] | ||
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[[Category: substrate channeling]] | [[Category: substrate channeling]] | ||
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Revision as of 13:48, 30 October 2007
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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 ... [(full description)]
About this StructureAbout this Structure
1OFD is a [Single protein] structure of sequence from [Synechocystis sp.] with FMN, F3S and AKG as [ligands]. Active as [Glutamate synthase (ferredoxin)], with EC number [1.4.7.1]. Structure known Active Site: AC1. 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
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