1lm1: Difference between revisions
New page: left|200px<br /><applet load="1lm1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lm1, resolution 2.80Å" /> '''Structural studies o... |
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[[Image:1lm1.jpg|left|200px]]<br /><applet load="1lm1" size=" | [[Image:1lm1.jpg|left|200px]]<br /><applet load="1lm1" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1lm1, resolution 2.80Å" /> | caption="1lm1, resolution 2.80Å" /> | ||
'''Structural studies on the synchronization of catalytic centers in glutamate synthase: native enzyme'''<br /> | '''Structural studies on the synchronization of catalytic centers in glutamate synthase: native enzyme'''<br /> | ||
==Overview== | ==Overview== | ||
The complex iron-sulfur flavoprotein glutamate synthase (GltS) plays a | The complex iron-sulfur flavoprotein glutamate synthase (GltS) plays a prominent role in ammonia assimilation in bacteria, yeasts, and plants. GltS catalyzes the formation of two molecules of l-glutamate from 2-oxoglutarate and l-glutamine via intramolecular channeling of ammonia. GltS has the impressive ability of synchronizing its distinct catalytic centers to avoid wasteful consumption of l-glutamine. We have determined the crystal structure of the ferredoxin-dependent GltS in several ligation and redox states. The structures reveal the crucial elements in the synchronization between the glutaminase site and the 2-iminoglutarate reduction site. The structural data combined with the catalytic properties of GltS indicate that binding of ferredoxin and 2-oxoglutarate to the FMN-binding domain of GltS induce a conformational change in the loop connecting the two catalytic centers. The rearrangement induces a shift in the catalytic elements of the amidotransferase domain, such that it becomes activated. This machinery, over a distance of more than 30 A, controls the ability of the enzyme to bind and hydrolyze the ammonia-donating substrate l-glutamine. | ||
==About this Structure== | ==About this Structure== | ||
1LM1 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 ACT, FMN and F3S 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] Full crystallographic information is available from [http:// | 1LM1 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 <scene name='pdbligand=ACT:'>ACT</scene>, <scene name='pdbligand=FMN:'>FMN</scene> and <scene name='pdbligand=F3S:'>F3S</scene> 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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LM1 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Synechocystis sp.]] | [[Category: Synechocystis sp.]] | ||
[[Category: Bossi, R | [[Category: Bossi, R T.]] | ||
[[Category: Curti, B.]] | [[Category: Curti, B.]] | ||
[[Category: Ferrari, D.]] | [[Category: Ferrari, D.]] | ||
[[Category: Florencio, F | [[Category: Florencio, F J.]] | ||
[[Category: Heuvel, R | [[Category: Heuvel, R H.van Den.]] | ||
[[Category: Mattevi, A.]] | [[Category: Mattevi, A.]] | ||
[[Category: Ravasio, S.]] | [[Category: Ravasio, S.]] | ||
[[Category: Vanoni, M | [[Category: Vanoni, M A.]] | ||
[[Category: ACT]] | [[Category: ACT]] | ||
[[Category: F3S]] | [[Category: F3S]] | ||
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[[Category: glutamate synthase]] | [[Category: glutamate synthase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:46:13 2008'' | ||
Revision as of 14:46, 21 February 2008
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Structural studies on the synchronization of catalytic centers in glutamate synthase: native enzyme
OverviewOverview
The complex iron-sulfur flavoprotein glutamate synthase (GltS) plays a prominent role in ammonia assimilation in bacteria, yeasts, and plants. GltS catalyzes the formation of two molecules of l-glutamate from 2-oxoglutarate and l-glutamine via intramolecular channeling of ammonia. GltS has the impressive ability of synchronizing its distinct catalytic centers to avoid wasteful consumption of l-glutamine. We have determined the crystal structure of the ferredoxin-dependent GltS in several ligation and redox states. The structures reveal the crucial elements in the synchronization between the glutaminase site and the 2-iminoglutarate reduction site. The structural data combined with the catalytic properties of GltS indicate that binding of ferredoxin and 2-oxoglutarate to the FMN-binding domain of GltS induce a conformational change in the loop connecting the two catalytic centers. The rearrangement induces a shift in the catalytic elements of the amidotransferase domain, such that it becomes activated. This machinery, over a distance of more than 30 A, controls the ability of the enzyme to bind and hydrolyze the ammonia-donating substrate l-glutamine.
About this StructureAbout this Structure
1LM1 is a Single protein structure of sequence from Synechocystis sp. with , and as ligands. Active as Glutamate synthase (ferredoxin), with EC number 1.4.7.1 Full crystallographic information is available from OCA.
ReferenceReference
Structural studies on the synchronization of catalytic centers in glutamate synthase., van den Heuvel RH, Ferrari D, Bossi RT, Ravasio S, Curti B, Vanoni MA, Florencio FJ, Mattevi A, J Biol Chem. 2002 Jul 5;277(27):24579-83. Epub 2002 Apr 19. PMID:11967268
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