2de5: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
<StructureSection load='2de5' size='340' side='right'caption='[[2de5]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='2de5' size='340' side='right'caption='[[2de5]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2de5]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2de5]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Janthinobacterium Janthinobacterium] and [https://en.wikipedia.org/wiki/Pseudomonas_resinovorans Pseudomonas resinovorans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DE5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DE5 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</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=2de5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2de5 OCA], [https://pdbe.org/2de5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2de5 RCSB], [https://www.ebi.ac.uk/pdbsum/2de5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2de5 ProSAT]</span></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=2de5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2de5 OCA], [https://pdbe.org/2de5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2de5 RCSB], [https://www.ebi.ac.uk/pdbsum/2de5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2de5 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q84II6_JANS3 Q84II6_JANS3] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 34: | Line 36: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Janthinobacterium]] | [[Category: Janthinobacterium]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Pseudomonas resinovorans]] | ||
[[Category: | [[Category: Ashikawa Y]] | ||
[[Category: | [[Category: Nojiri H]] | ||
Latest revision as of 11:25, 25 October 2023
Crystal structure of the electron transfer complex between oxygenase and ferredoxin in carbazole 1,9a-dioxygenaseCrystal structure of the electron transfer complex between oxygenase and ferredoxin in carbazole 1,9a-dioxygenase
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCarbazole 1,9a-dioxygenase (CARDO), a member of the Rieske nonheme iron oxygenase system (ROS), consists of a terminal oxygenase (CARDO-O) and electron transfer components (ferredoxin [CARDO-F] and ferredoxin reductase [CARDO-R]). We determined the crystal structures of the nonreduced, reduced, and substrate-bound binary complexes of CARDO-O with its electron donor, CARDO-F, at 1.9, 1.8, and 2.0 A resolutions, respectively. These structures provide the first structure-based interpretation of intercomponent electron transfer between two Rieske [2Fe-2S] clusters of ferredoxin and oxygenase in ROS. Three molecules of CARDO-F bind to the subunit boundary of one CARDO-O trimeric molecule, and specific binding created by electrostatic and hydrophobic interactions with conformational changes suitably aligns the two Rieske clusters for electron transfer. Additionally, conformational changes upon binding carbazole resulted in the closure of a lid over the substrate-binding pocket, thereby seemingly trapping carbazole at the substrate-binding site. Electron transfer complex formation between oxygenase and ferredoxin components in Rieske nonheme iron oxygenase system.,Ashikawa Y, Fujimoto Z, Noguchi H, Habe H, Omori T, Yamane H, Nojiri H Structure. 2006 Dec;14(12):1779-89. PMID:17161368[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||