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4doy

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Current revision (08:48, 20 March 2024) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4doy]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodococcus_erythropolis_XP Rhodococcus erythropolis XP]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DOY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DOY FirstGlance]. <br>
<table><tr><td colspan='2'>[[4doy]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodococcus_erythropolis_XP Rhodococcus erythropolis XP]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DOY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DOY FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.789&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=4doy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4doy OCA], [https://pdbe.org/4doy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4doy RCSB], [https://www.ebi.ac.uk/pdbsum/4doy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4doy 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=4doy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4doy OCA], [https://pdbe.org/4doy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4doy RCSB], [https://www.ebi.ac.uk/pdbsum/4doy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4doy ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/DSZC_RHOSH DSZC_RHOSH]] Catalyzes the first step of the '4S' desulfurization pathway that removes covalently bound sulfur from dibenzothiophene (DBT) without breaking carbon-carbon bonds. Sulfur dioxygenase which converts DBT to DBT-sulfone (DBTO2 or DBT 5,5-dioxide) in a stepwise manner.<ref>PMID:16820450</ref>
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[https://www.uniprot.org/uniprot/DSZC_RHOSH DSZC_RHOSH] Catalyzes the first step of the '4S' desulfurization pathway that removes covalently bound sulfur from dibenzothiophene (DBT) without breaking carbon-carbon bonds. Sulfur dioxygenase which converts DBT to DBT-sulfone (DBTO2 or DBT 5,5-dioxide) in a stepwise manner.<ref>PMID:16820450</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The dibenzothiophene (DBT) monooxygenase DszC, which is the key initiating enzyme in ''4S'' metabolic pathway, catalyzes sequential sulphoxidation reaction of DBT to DBT sulfoxide (DBTO), then DBT sulfone (DBTO2 ). Here, we report the crystal structure of DszC from Rhodococcus sp. XP at 1.79 A. Intriguingly, two distinct conformations occur in the flexible lid loops adjacent to the active site (residue 280-295, between alpha9 and alpha10). They are named ''open'' and ''closed'' state respectively, and might show the status of the free and ligand-bound DszC. The molecular docking results suggest that the reduced FMN reacts with an oxygen molecule at C4a position of the isoalloxazine ring, producing the C4a-(hydro)peroxyflavin intermediate which is stabilized by H391 and S163. H391 may contribute to the formation of the C4a-(hydro)peroxyflavin by acting as a proton donor to the proximal peroxy oxygen, and it might also be involved in the protonation process of the C4a-(hydro)xyflavin. Site-directed mutagenesis study shows that mutations in the residues involved either in catalysis or in flavin or substrate-binding result in a complete loss of enzyme activity, suggesting that the accurate positions of flavin and substrate are crucial for the enzyme activity. (c) Proteins 2014;. (c) 2014 Wiley Periodicals, Inc.
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Crystal structure of DszC from Rhodococcus sp. XP at 1.79 A,Liu S, Zhang C, Su T, Wei T, Zhu D, Wang K, Huang Y, Dong Y, Yin K, Xu S, Xu P, Gu L Proteins. 2014 Jan 28. doi: 10.1002/prot.24525. PMID:24470304<ref>PMID:24470304</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4doy" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>

Current revision

Crystal structure of Dibenzothiophene desulfurization enzyme C

PDB ID 4doy

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