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| | ==Structural and functional characterization of OleP in complex with 6DEB in PEG== | | ==Structural and functional characterization of OleP in complex with 6DEB in PEG== |
| - | <StructureSection load='5mnv' size='340' side='right' caption='[[5mnv]], [[Resolution|resolution]] 2.97Å' scene=''> | + | <StructureSection load='5mnv' size='340' side='right'caption='[[5mnv]], [[Resolution|resolution]] 2.97Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5mnv]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/"actinomyces_antibioticus"_waksman_and_woodruff_1941 "actinomyces antibioticus" waksman and woodruff 1941]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MNV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MNV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5mnv]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_antibioticus Streptomyces antibioticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MNV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MNV FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DEB:6-DEOXYERYTHRONOLIDE+B'>DEB</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.97Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">oleP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1890 "Actinomyces antibioticus" Waksman and Woodruff 1941])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DEB:6-DEOXYERYTHRONOLIDE+B'>DEB</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5mnv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mnv OCA], [http://pdbe.org/5mnv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mnv RCSB], [http://www.ebi.ac.uk/pdbsum/5mnv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mnv 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=5mnv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mnv OCA], [https://pdbe.org/5mnv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mnv RCSB], [https://www.ebi.ac.uk/pdbsum/5mnv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mnv ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q59819_STRAT Q59819_STRAT] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Actinomyces antibioticus waksman and woodruff 1941]] | + | [[Category: Large Structures]] |
| - | [[Category: Montemiglio, L C]] | + | [[Category: Streptomyces antibioticus]] |
| - | [[Category: Parisi, G]] | + | [[Category: Montemiglio LC]] |
| - | [[Category: Savino, C]] | + | [[Category: Parisi G]] |
| - | [[Category: Cytochrome]] | + | [[Category: Savino C]] |
| - | [[Category: Epoxidase]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: P450]]
| + | |
| Structural highlights
Function
Q59819_STRAT
Publication Abstract from PubMed
The regulation of cytochrome P450 activity is often achieved by structural transitions induced by substrate binding. We describe the conformational transition experienced upon binding by the P450 OleP, an epoxygenase involved in oleandomycin biosynthesis. OleP bound to the substrate analog 6DEB crystallized in 2 forms: one with an ensemble of open and closed conformations in the asymmetric unit and another with only the closed conformation. Characterization of OleP-6DEB binding kinetics, also using the P450 inhibitor clotrimazole, unveiled a complex binding mechanism that involves slow conformational rearrangement with the accumulation of a spectroscopically detectable intermediate where 6DEB is bound to open OleP. Data reported herein provide structural snapshots of key precatalytic steps in the OleP reaction and explain how structural rearrangements induced by substrate binding regulate activity.-Parisi, G., Montemiglio, L. C., Giuffre, A., Macone, A., Scaglione, A., Cerutti, G., Exertier, C., Savino, C., Vallone, B. Substrate-induced conformational change in cytochrome P450 OleP.
Substrate-induced conformational change in cytochrome P450 OleP.,Parisi G, Montemiglio LC, Giuffre A, Macone A, Scaglione A, Cerutti G, Exertier C, Savino C, Vallone B FASEB J. 2018 Sep 12:fj201800450RR. doi: 10.1096/fj.201800450RR. PMID:30207799[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Parisi G, Montemiglio LC, Giuffre A, Macone A, Scaglione A, Cerutti G, Exertier C, Savino C, Vallone B. Substrate-induced conformational change in cytochrome P450 OleP. FASEB J. 2018 Sep 12:fj201800450RR. doi: 10.1096/fj.201800450RR. PMID:30207799 doi:http://dx.doi.org/10.1096/fj.201800450RR
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