7c3a: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Ferredoxin reductase in carbazole 1,9a-dioxygenase== | ==Ferredoxin reductase in carbazole 1,9a-dioxygenase== | ||
<StructureSection load='7c3a' size='340' side='right'caption='[[7c3a]]' scene=''> | <StructureSection load='7c3a' size='340' side='right'caption='[[7c3a]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7C3A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7C3A FirstGlance]. <br> | <table><tr><td colspan='2'>[[7c3a]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Jans3 Jans3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7C3A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7C3A FirstGlance]. <br> | ||
</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=7c3a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7c3a OCA], [https://pdbe.org/7c3a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7c3a RCSB], [https://www.ebi.ac.uk/pdbsum/7c3a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7c3a ProSAT]</span></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">carAd ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=213804 JANS3])</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=7c3a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7c3a OCA], [https://pdbe.org/7c3a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7c3a RCSB], [https://www.ebi.ac.uk/pdbsum/7c3a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7c3a ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Carbazole 1,9a-dioxygenase (CARDO), which consists of an oxygenase component and the electron-transport components ferredoxin (CARDO-F) and ferredoxin reductase (CARDO-R), is a Rieske nonheme iron oxygenase (RO). ROs are classified into five subclasses (IA, IB, IIA, IIB and III) based on their number of constituents and the nature of their redox centres. In this study, two types of crystal structure (type I and type II) were resolved of the class III CARDO-R from Janthinobacterium sp. J3 (CARDO-RJ3). Superimposition of the type I and type II structures revealed the absence of flavin adenine dinucleotide (FAD) in the type II structure along with significant conformational changes to the FAD-binding domain and the C-terminus, including movements to fill the space in which FAD had been located. Docking simulation of NADH into the FAD-bound form of CARDO-RJ3 suggested that shifts of the residues at the C-terminus caused the nicotinamide moiety to approach the N5 atom of FAD, which might facilitate electron transfer between the redox centres. Differences in domain arrangement were found compared with RO reductases from the ferredoxin-NADP reductase family, suggesting that these differences correspond to differences in the structures of their redox partners ferredoxin and terminal oxygenase. The results of docking simulations with the redox partner class III CARDO-F from Pseudomonas resinovorans CA10 suggested that complex formation suitable for efficient electron transfer is stabilized by electrostatic attraction and complementary shapes of the interacting regions. | |||
Crystal structure of the ferredoxin reductase component of carbazole 1,9a-dioxygenase from Janthinobacterium sp. J3.,Ashikawa Y, Fujimoto Z, Inoue K, Yamane H, Nojiri H Acta Crystallogr D Struct Biol. 2021 Jul 1;77(Pt 7):921-932. doi:, 10.1107/S2059798321005040. Epub 2021 Jun 18. PMID:34196618<ref>PMID:34196618</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7c3a" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Jans3]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Ashikawa Y]] | [[Category: Ashikawa, Y]] | ||
[[Category: Fujimoto Z]] | [[Category: Fujimoto, Z]] | ||
[[Category: Nojiri H]] | [[Category: Nojiri, H]] | ||
[[Category: Carbazole]] | |||
[[Category: Electron transfer]] | |||
[[Category: Ferredoxin]] | |||
[[Category: Oxidoreductase]] | |||
[[Category: Rieske non-heme iron oxygenase]] | |||
Revision as of 13:05, 14 July 2021
Ferredoxin reductase in carbazole 1,9a-dioxygenaseFerredoxin reductase in carbazole 1,9a-dioxygenase
Structural highlights
Publication Abstract from PubMedCarbazole 1,9a-dioxygenase (CARDO), which consists of an oxygenase component and the electron-transport components ferredoxin (CARDO-F) and ferredoxin reductase (CARDO-R), is a Rieske nonheme iron oxygenase (RO). ROs are classified into five subclasses (IA, IB, IIA, IIB and III) based on their number of constituents and the nature of their redox centres. In this study, two types of crystal structure (type I and type II) were resolved of the class III CARDO-R from Janthinobacterium sp. J3 (CARDO-RJ3). Superimposition of the type I and type II structures revealed the absence of flavin adenine dinucleotide (FAD) in the type II structure along with significant conformational changes to the FAD-binding domain and the C-terminus, including movements to fill the space in which FAD had been located. Docking simulation of NADH into the FAD-bound form of CARDO-RJ3 suggested that shifts of the residues at the C-terminus caused the nicotinamide moiety to approach the N5 atom of FAD, which might facilitate electron transfer between the redox centres. Differences in domain arrangement were found compared with RO reductases from the ferredoxin-NADP reductase family, suggesting that these differences correspond to differences in the structures of their redox partners ferredoxin and terminal oxygenase. The results of docking simulations with the redox partner class III CARDO-F from Pseudomonas resinovorans CA10 suggested that complex formation suitable for efficient electron transfer is stabilized by electrostatic attraction and complementary shapes of the interacting regions. Crystal structure of the ferredoxin reductase component of carbazole 1,9a-dioxygenase from Janthinobacterium sp. J3.,Ashikawa Y, Fujimoto Z, Inoue K, Yamane H, Nojiri H Acta Crystallogr D Struct Biol. 2021 Jul 1;77(Pt 7):921-932. doi:, 10.1107/S2059798321005040. Epub 2021 Jun 18. PMID:34196618[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||