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1vck

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Revision as of 14:15, 10 September 2015

Crystal structure of ferredoxin component of carbazole 1,9a-dioxygenase of Pseudomonas resinovorans strain CA10

Structural highlights

1vck is a 1 chain structure with sequence from Atcc 14235. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[CARAC_PSERE] Part of the multicomponent carbazole 1,9a-dioxygenase (CARDO), that converts carbazole (CAR) into 2-aminobiphenyl-2,3-diol. Acts as a mediator in the electron transfer from CarAd to CarAa.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

Crystal structure of the ferredoxin component of carbazole 1,9a-dioxygenase of Pseudomonas resinovorans strain CA10, a novel Rieske non-heme iron oxygenase system.,Nam JW, Noguchi H, Fujimoto Z, Mizuno H, Ashikawa Y, Abo M, Fushinobu S, Kobashi N, Wakagi T, Iwata K, Yoshida T, Habe H, Yamane H, Omori T, Nojiri H Proteins. 2005 Mar 1;58(4):779-89. PMID:15645447^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Sato SI, Nam JW, Kasuga K, Nojiri H, Yamane H, Omori T. Identification and characterization of genes encoding carbazole 1,9a-dioxygenase in Pseudomonas sp. strain CA10. J Bacteriol. 1997 Aug;179(15):4850-8. PMID:9244274
↑ Nam JW, Nojiri H, Noguchi H, Uchimura H, Yoshida T, Habe H, Yamane H, Omori T. Purification and characterization of carbazole 1,9a-dioxygenase, a three-component dioxygenase system of Pseudomonas resinovorans strain CA10. Appl Environ Microbiol. 2002 Dec;68(12):5882-90. PMID:12450807
↑ Nam JW, Noguchi H, Fujimoto Z, Mizuno H, Ashikawa Y, Abo M, Fushinobu S, Kobashi N, Wakagi T, Iwata K, Yoshida T, Habe H, Yamane H, Omori T, Nojiri H. Crystal structure of the ferredoxin component of carbazole 1,9a-dioxygenase of Pseudomonas resinovorans strain CA10, a novel Rieske non-heme iron oxygenase system. Proteins. 2005 Mar 1;58(4):779-89. PMID:15645447 doi:10.1002/prot.20374

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1vck"

@@ Line 2: / Line 2: @@
 <StructureSection load='1vck' size='340' side='right' caption='[[1vck]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1vck]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_resinovorans Pseudomonas resinovorans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VCK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1VCK FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1vck]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_14235 Atcc 14235]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VCK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1VCK FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=H2S:HYDROSULFURIC+ACID'>H2S</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vck OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1vck RCSB], [http://www.ebi.ac.uk/pdbsum/1vck PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vck OCA], [http://pdbe.org/1vck PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1vck RCSB], [http://www.ebi.ac.uk/pdbsum/1vck PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/Q8GI16_PSERE Q8GI16_PSERE]] Part of the multicomponent carbazole 1,9a-dioxygenase (CARDO), that converts carbazole (CAR) into 2-aminobiphenyl-2,3-diol. Acts as a mediator in the electron transfer from CarAd to CarAa.<ref>PMID:9244274</ref> <ref>PMID:12450807</ref>
+[[http://www.uniprot.org/uniprot/CARAC_PSERE CARAC_PSERE]] Part of the multicomponent carbazole 1,9a-dioxygenase (CARDO), that converts carbazole (CAR) into 2-aminobiphenyl-2,3-diol. Acts as a mediator in the electron transfer from CarAd to CarAa.<ref>PMID:9244274</ref> <ref>PMID:12450807</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 26: / Line 26: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1vck" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 34: / Line 35: @@
 __TOC__
 </StructureSection>
-[[Category: Pseudomonas resinovorans]]
+[[Category: Atcc 14235]]
 [[Category: Fujiomoto, Z]]
 [[Category: Fushinobu, S]]

1vck

From Proteopedia

Revision as of 14:15, 10 September 2015

Crystal structure of ferredoxin component of carbazole 1,9a-dioxygenase of Pseudomonas resinovorans strain CA10

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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