View source for 1vck


==Crystal structure of ferredoxin component of carbazole 1,9a-dioxygenase of Pseudomonas resinovorans strain CA10==
<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 [https://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 [https://proteopedia.org/fgij/fg.htm?mol=1VCK FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=1vck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vck OCA], [https://pdbe.org/1vck PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vck RCSB], [https://www.ebi.ac.uk/pdbsum/1vck PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vck ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CARAC_METRE CARAC_METRE] 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:12450807</ref> <ref>PMID:9244274</ref> 
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vc/1vck_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1vck ConSurf].
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== 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<ref>PMID:15645447</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1vck" style="background-color:#fffaf0;"></div>

==See Also==
*[[Dioxygenase 3D structures|Dioxygenase 3D structures]]
*[[Ferredoxin 3D structures|Ferredoxin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas resinovorans]]
[[Category: Fujiomoto Z]]
[[Category: Fushinobu S]]
[[Category: Habe H]]
[[Category: Iwata K]]
[[Category: Kobashi N]]
[[Category: Mizuno H]]
[[Category: Nam J-W]]
[[Category: Noguchi H]]
[[Category: Nojiri H]]
[[Category: Omori T]]
[[Category: Yamane H]]
[[Category: Yoshida T]]