1llw: Difference between revisions

Line 1:

[[Image:1llw.gif|left|200px]]<br /><applet load="1llw" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1llw.gif|left|200px]]<br /><applet load="1llw" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1llw, resolution 2.70Å" />

'''Structural studies on the synchronization of catalytic centers in glutamate synthase: complex with 2-oxoglutarate'''<br />

==Overview==

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.

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==

1LLW 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] Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1LLW OCA].

1LLW 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=FMN:'>FMN</scene>, <scene name='pdbligand=F3S:'>F3S</scene> and <scene name='pdbligand=AKG:'>AKG</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=1LLW OCA].

==Reference==

Line 14:

[[Category: Single protein]]

[[Category: Synechocystis sp.]]

[[Category: Bossi, R.T.]]

[[Category: Bossi, R T.]]

[[Category: Curti, B.]]

[[Category: Ferrari, D.]]

[[Category: Florencio, F.J.]]

[[Category: Florencio, F J.]]

[[Category: Heuvel, R.H.van.den.]]

[[Category: Heuvel, R H.van den.]]

[[Category: Mattevi, A.]]

[[Category: Ravasio, S.]]

[[Category: Vanoni, M.A.]]

[[Category: Vanoni, M A.]]

[[Category: AKG]]

[[Category: F3S]]

Line 29:

[[Category: ntn amidotransferase]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:46:10 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1llw.gif|left|200px]]<br /><applet load="1llw" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1llw.gif|left|200px]]<br /><applet load="1llw" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1llw, resolution 2.70&Aring;" />
 '''Structural studies on the synchronization of catalytic centers in glutamate synthase: complex with 2-oxoglutarate'''<br />
 ==Overview==
-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.
+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==
-LLW 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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LLW OCA].
+LLW 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=FMN:'>FMN</scene>, <scene name='pdbligand=F3S:'>F3S</scene> and <scene name='pdbligand=AKG:'>AKG</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=1LLW OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Synechocystis sp.]]
-[[Category: Bossi, R.T.]]
+[[Category: Bossi, R T.]]
 [[Category: Curti, B.]]
 [[Category: Ferrari, D.]]
-[[Category: Florencio, F.J.]]
+[[Category: Florencio, F J.]]
-[[Category: Heuvel, R.H.van.den.]]
+[[Category: Heuvel, R H.van den.]]
 [[Category: Mattevi, A.]]
 [[Category: Ravasio, S.]]
-[[Category: Vanoni, M.A.]]
+[[Category: Vanoni, M A.]]
 [[Category: AKG]]
 [[Category: F3S]]
@@ Line 29: / Line 29: @@
 [[Category: ntn amidotransferase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:39:50 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:46:10 2008''