7dls
From Proteopedia
(Difference between revisions)
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==Cytochrome P450 (CYP105D18) complex with papaverine== | ==Cytochrome P450 (CYP105D18) complex with papaverine== | ||
| - | <StructureSection load='7dls' size='340' side='right'caption='[[7dls]]' scene=''> | + | <StructureSection load='7dls' size='340' side='right'caption='[[7dls]], [[Resolution|resolution]] 2.06Å' 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=7DLS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DLS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7dls]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_31255 Atcc 31255]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DLS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DLS 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=7dls FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dls OCA], [https://pdbe.org/7dls PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dls RCSB], [https://www.ebi.ac.uk/pdbsum/7dls PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dls 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=EV1:1-(3,4-DIMETHOXYBENZYL)-6,7-DIMETHOXYISOQUINOLINE'>EV1</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr> |
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[7di3|7di3]]</div></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SLA_5925 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=39478 ATCC 31255])</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=7dls FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dls OCA], [https://pdbe.org/7dls PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dls RCSB], [https://www.ebi.ac.uk/pdbsum/7dls PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dls ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The bacterial CYP105 family is involved in secondary metabolite biosynthetic pathways and plays essential roles in the biotransformation of xenobiotics. This study investigates the newly identified H2O2-mediated CYP105D18 from Streptomyces laurentii as the first bacterial CYP for N-oxidation. The catalytic efficiency of CYP105D18 for papaverine N-oxidation was 1.43 s(-1) microM (-1). The heme oxidation rate (k) was low (<0.3 min(-1)) in the presence of 200 mM H2O2. This high H2O2 tolerance capacity of CYP105D18 led to higher turnover prior to heme oxidation. Additionally, the high-resolution papaverine complexed structure and substrate-free structure of CYP105D18 were determined. Structural analysis and activity assay results revealed that CYP105D18 had a strong substrate preference for papaverine because of its bendable structure. These findings establish a basis for biotechnological applications of CYP105D18 in the pharmaceutical and medicinal industries. | ||
| + | |||
| + | Characterization of high-H2O2-tolerant bacterial cytochrome P450 CYP105D18: insights into papaverine N-oxidation.,Pardhe BD, Do H, Jeong CS, Kim KH, Lee JH, Oh TJ IUCrJ. 2021 Jun 29;8(Pt 4):684-694. doi: 10.1107/S2052252521005522. eCollection, 2021 Jul 1. PMID:34258016<ref>PMID:34258016</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7dls" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Atcc 31255]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Do H]] | + | [[Category: Do, H]] |
| - | [[Category: Lee | + | [[Category: Lee, J H]] |
| + | [[Category: Chemical modification]] | ||
| + | [[Category: Eukaryotic cytochrome p450]] | ||
| + | [[Category: Heme oxidation]] | ||
| + | [[Category: Papaverine n-oxide]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 10:47, 28 July 2021
Cytochrome P450 (CYP105D18) complex with papaverine
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