6wfl: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Camphor soaked P450cam D251E== | ==Camphor soaked P450cam D251E== | ||
<StructureSection load='6wfl' size='340' side='right'caption='[[6wfl]]' scene=''> | <StructureSection load='6wfl' size='340' side='right'caption='[[6wfl]], [[Resolution|resolution]] 1.60Å' 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=6WFL OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6WFL FirstGlance]. <br> | <table><tr><td colspan='2'>[[6wfl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6WFL OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6WFL FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6wfl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wfl OCA], [http://pdbe.org/6wfl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6wfl RCSB], [http://www.ebi.ac.uk/pdbsum/6wfl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6wfl 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=CAH:5-EXO-HYDROXYCAMPHOR'>CAH</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6we6|6we6]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">camC, cyp101 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=303 "Bacillus fluorescens putidus" Flugge 1886])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Camphor_5-monooxygenase Camphor 5-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.15.1 1.14.15.1] </span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6wfl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wfl OCA], [http://pdbe.org/6wfl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6wfl RCSB], [http://www.ebi.ac.uk/pdbsum/6wfl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6wfl ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/CPXA_PSEPU CPXA_PSEPU]] Involved in a camphor oxidation system. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Cytochrome P450s are amongst nature's most powerful catalysts. Their ability to activate molecular dioxygen to form high-valent ferryl intermediates (Compounds I and II) enables a wide array of chemistries ranging from simple epoxidations to more complicated C-H bond oxidation. Oxygen activation is achieved by reduction of the ferrous dioxygen complex, which requires electron transfer from a redox partner and subsequent double protonation to yield a water molecule and a ferryl porphyrin pi-cation radical (Compound I). Previous studies on the CYP101 family of cytochrome P450s demonstrated the importance of the conserved active site Asp25X residue in this protonation event, although its precise role is still yet to be unraveled. To further explore the origin of protons in oxygen activation, we analyzed the effects of an Asp to Glu mutation at the 25X position in P450cam and in CYP101D1. This mutation inactivates P450cam but not CYP101D1. A series of mutagenic, crystallographic, kinetic and molecular dynamics studies indicate that this mutation locks P450cam into a closed inactive conformation. In CYP101D1 the D259E mutant changes the rate limiting step to reduction of the P450-oxy complex thus opening a window into the critical proton coupled electron step in P450 catalysis. | |||
The Proton Relay Network in the Bacterial P450s: CYP101A1 and CYP101D1.,Amaya JA, Batabyal D, Poulos TL Biochemistry. 2020 Jun 23. doi: 10.1021/acs.biochem.0c00329. PMID:32574066<ref>PMID:32574066</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6wfl" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bacillus fluorescens putidus flugge 1886]] | |||
[[Category: Camphor 5-monooxygenase]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Amaya | [[Category: Amaya, J A]] | ||
[[Category: Batabyal D]] | [[Category: Batabyal, D]] | ||
[[Category: Poulos | [[Category: Poulos, T L]] | ||
[[Category: Camphor]] | |||
[[Category: D251e]] | |||
[[Category: Oxidoreductase]] | |||
[[Category: P450cam]] | |||
[[Category: Pdr]] | |||
[[Category: Pdx]] | |||
Revision as of 14:36, 26 August 2020
Camphor soaked P450cam D251ECamphor soaked P450cam D251E
Structural highlights
Function[CPXA_PSEPU] Involved in a camphor oxidation system. Publication Abstract from PubMedCytochrome P450s are amongst nature's most powerful catalysts. Their ability to activate molecular dioxygen to form high-valent ferryl intermediates (Compounds I and II) enables a wide array of chemistries ranging from simple epoxidations to more complicated C-H bond oxidation. Oxygen activation is achieved by reduction of the ferrous dioxygen complex, which requires electron transfer from a redox partner and subsequent double protonation to yield a water molecule and a ferryl porphyrin pi-cation radical (Compound I). Previous studies on the CYP101 family of cytochrome P450s demonstrated the importance of the conserved active site Asp25X residue in this protonation event, although its precise role is still yet to be unraveled. To further explore the origin of protons in oxygen activation, we analyzed the effects of an Asp to Glu mutation at the 25X position in P450cam and in CYP101D1. This mutation inactivates P450cam but not CYP101D1. A series of mutagenic, crystallographic, kinetic and molecular dynamics studies indicate that this mutation locks P450cam into a closed inactive conformation. In CYP101D1 the D259E mutant changes the rate limiting step to reduction of the P450-oxy complex thus opening a window into the critical proton coupled electron step in P450 catalysis. The Proton Relay Network in the Bacterial P450s: CYP101A1 and CYP101D1.,Amaya JA, Batabyal D, Poulos TL Biochemistry. 2020 Jun 23. doi: 10.1021/acs.biochem.0c00329. PMID:32574066[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||||||