1vck: Difference between revisions

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

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

caption="1vck, resolution 1.90Å" />

'''Crystal structure of ferredoxin component of carbazole 1,9a-dioxygenase of Pseudomonas resinovorans strain CA10'''<br />

==Overview==

The carbazole 1,9a-dioxygenase (CARDO) system of Pseudomonas resinovorans, strain CA10 catalyzes the dioxygenation of carbazole; the 9aC carbon bonds, to a nitrogen atom and its adjacent 1C carbon as the initial reaction in, the mineralization pathway. The CARDO system is composed of ferredoxin, reductase (CarAd), ferredoxin (CarAc), and terminal oxygenase (CarAa)., CarAc acts as a mediator in the electron transfer from CarAd to CarAa. To, understand the structural basis of the protein-protein interactions during, electron transport in the CARDO system, the crystal structure of CarAc was, determined at 1.9 A resolution by molecular replacement using the, structure of BphF, the biphenyl 2,3-dioxygenase ferredoxin from, Burkholderia cepacia strain LB400 as a search model. CarAc is composed of, three beta-sheets, and the structure can be divided into two domains, a, cluster-binding domain and a basal domain. The Rieske [2Fe-2S] cluster is, located at the tip of the cluster-binding domain, where it is exposed to, solvent. While the overall folding of CarAc and BphF is strongly, conserved, the properties of their surfaces are very different from each, other. The structure of the cluster-binding domain of CarAc is more, compact and protruding than that of BphF, and the distribution of electric, charge on its molecular surface is very different. Such differences are, thought to explain why these ferredoxins can act as electron mediators in, respective electron transport chains composed of different-featured, components.

The carbazole 1,9a-dioxygenase (CARDO) system of Pseudomonas resinovorans strain CA10 catalyzes the dioxygenation of carbazole; the 9aC carbon bonds to a nitrogen atom and its adjacent 1C carbon as the initial reaction in the mineralization pathway. The CARDO system is composed of ferredoxin reductase (CarAd), ferredoxin (CarAc), and terminal oxygenase (CarAa). CarAc acts as a mediator in the electron transfer from CarAd to CarAa. To understand the structural basis of the protein-protein interactions during electron transport in the CARDO system, the crystal structure of CarAc was determined at 1.9 A resolution by molecular replacement using the structure of BphF, the biphenyl 2,3-dioxygenase ferredoxin from Burkholderia cepacia strain LB400 as a search model. CarAc is composed of three beta-sheets, and the structure can be divided into two domains, a cluster-binding domain and a basal domain. The Rieske [2Fe-2S] cluster is located at the tip of the cluster-binding domain, where it is exposed to solvent. While the overall folding of CarAc and BphF is strongly conserved, the properties of their surfaces are very different from each other. The structure of the cluster-binding domain of CarAc is more compact and protruding than that of BphF, and the distribution of electric charge on its molecular surface is very different. Such differences are thought to explain why these ferredoxins can act as electron mediators in respective electron transport chains composed of different-featured components.

==About this Structure==

1VCK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_resinovorans Pseudomonas resinovorans] with FE, FES and S as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1VCK OCA].

1VCK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_resinovorans Pseudomonas resinovorans] with <scene name='pdbligand=FE:'>FE</scene>, <scene name='pdbligand=FES:'>FES</scene> and <scene name='pdbligand=S:'>S</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VCK OCA].

==Reference==

Line 19:

[[Category: Kobashi, N.]]

[[Category: Mizuno, H.]]

[[Category: Nam, J.W.]]

[[Category: Nam, J W.]]

[[Category: Noguchi, H.]]

[[Category: Nojiri, H.]]

Line 36:

[[Category: rieske-type ferredoxin]]

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@@ Line 1: / Line 1: @@
-[[Image:1vck.gif|left|200px]]<br /><applet load="1vck" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1vck.gif|left|200px]]<br /><applet load="1vck" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1vck, resolution 1.90&Aring;" />
 '''Crystal structure of ferredoxin component of carbazole 1,9a-dioxygenase of Pseudomonas resinovorans strain CA10'''<br />
 ==Overview==
-The carbazole 1,9a-dioxygenase (CARDO) system of Pseudomonas resinovorans, strain CA10 catalyzes the dioxygenation of carbazole; the 9aC carbon bonds, to a nitrogen atom and its adjacent 1C carbon as the initial reaction in, the mineralization pathway. The CARDO system is composed of ferredoxin, reductase (CarAd), ferredoxin (CarAc), and terminal oxygenase (CarAa)., CarAc acts as a mediator in the electron transfer from CarAd to CarAa. To, understand the structural basis of the protein-protein interactions during, electron transport in the CARDO system, the crystal structure of CarAc was, determined at 1.9 A resolution by molecular replacement using the, structure of BphF, the biphenyl 2,3-dioxygenase ferredoxin from, Burkholderia cepacia strain LB400 as a search model. CarAc is composed of, three beta-sheets, and the structure can be divided into two domains, a, cluster-binding domain and a basal domain. The Rieske [2Fe-2S] cluster is, located at the tip of the cluster-binding domain, where it is exposed to, solvent. While the overall folding of CarAc and BphF is strongly, conserved, the properties of their surfaces are very different from each, other. The structure of the cluster-binding domain of CarAc is more, compact and protruding than that of BphF, and the distribution of electric, charge on its molecular surface is very different. Such differences are, thought to explain why these ferredoxins can act as electron mediators in, respective electron transport chains composed of different-featured, components.
+The carbazole 1,9a-dioxygenase (CARDO) system of Pseudomonas resinovorans strain CA10 catalyzes the dioxygenation of carbazole; the 9aC carbon bonds to a nitrogen atom and its adjacent 1C carbon as the initial reaction in the mineralization pathway. The CARDO system is composed of ferredoxin reductase (CarAd), ferredoxin (CarAc), and terminal oxygenase (CarAa). CarAc acts as a mediator in the electron transfer from CarAd to CarAa. To understand the structural basis of the protein-protein interactions during electron transport in the CARDO system, the crystal structure of CarAc was determined at 1.9 A resolution by molecular replacement using the structure of BphF, the biphenyl 2,3-dioxygenase ferredoxin from Burkholderia cepacia strain LB400 as a search model. CarAc is composed of three beta-sheets, and the structure can be divided into two domains, a cluster-binding domain and a basal domain. The Rieske [2Fe-2S] cluster is located at the tip of the cluster-binding domain, where it is exposed to solvent. While the overall folding of CarAc and BphF is strongly conserved, the properties of their surfaces are very different from each other. The structure of the cluster-binding domain of CarAc is more compact and protruding than that of BphF, and the distribution of electric charge on its molecular surface is very different. Such differences are thought to explain why these ferredoxins can act as electron mediators in respective electron transport chains composed of different-featured components.
 ==About this Structure==
-VCK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_resinovorans Pseudomonas resinovorans] with FE, FES and S as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1VCK OCA].
+VCK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_resinovorans Pseudomonas resinovorans] with <scene name='pdbligand=FE:'>FE</scene>, <scene name='pdbligand=FES:'>FES</scene> and <scene name='pdbligand=S:'>S</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VCK OCA].
 ==Reference==
@@ Line 19: / Line 19: @@
 [[Category: Kobashi, N.]]
 [[Category: Mizuno, H.]]
-[[Category: Nam, J.W.]]
+[[Category: Nam, J W.]]
 [[Category: Noguchi, H.]]
 [[Category: Nojiri, H.]]
@@ Line 36: / Line 36: @@
 [[Category: rieske-type ferredoxin]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 22:08:14 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:33:49 2008''