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==Crystal structure of Cytochrome P450cam-putidaredoxin complex==
==Crystal structure of Cytochrome P450cam-putidaredoxin complex==
<StructureSection load='4jws' size='340' side='right' caption='[[4jws]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
<StructureSection load='4jws' size='340' side='right'caption='[[4jws]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4jws]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JWS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JWS FirstGlance]. <br>
<table><tr><td colspan='2'>[[4jws]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JWS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JWS FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1N0:1,1-HEXANE-1,6-DIYLDIPYRROLIDINE-2,5-DIONE'>1N0</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</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]] 2.15&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4jwu|4jwu]], [[4jx1|4jx1]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1N0:1,1-HEXANE-1,6-DIYLDIPYRROLIDINE-2,5-DIONE'>1N0</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></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 Pseudomonas putida]), camB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=303 Pseudomonas putida])</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=4jws FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jws OCA], [https://pdbe.org/4jws PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jws RCSB], [https://www.ebi.ac.uk/pdbsum/4jws PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jws ProSAT]</span></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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4jws FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jws OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4jws RCSB], [http://www.ebi.ac.uk/pdbsum/4jws PDBsum]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/CPXA_PSEPU CPXA_PSEPU]] Involved in a camphor oxidation system. [[http://www.uniprot.org/uniprot/PUTX_PSEPU PUTX_PSEPU]] The oxidation of camphor by cytochrome P450-CAM requires the participation of a flavoprotein, putidaredoxin reductase, and an iron-sulfur protein, putidaredoxin, to mediate the transfer of electrons from NADH to P450 for oxygen activation.  
[https://www.uniprot.org/uniprot/CPXA_PSEPU CPXA_PSEPU] Involved in a camphor oxidation system.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 4jws" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Cytochrome P450|Cytochrome P450]]
*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]]
*[[Ferredoxin|Ferredoxin]]
*[[Ferredoxin 3D structures|Ferredoxin 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Camphor 5-monooxygenase]]
[[Category: Large Structures]]
[[Category: Pseudomonas putida]]
[[Category: Pseudomonas putida]]
[[Category: Li, H]]
[[Category: Li H]]
[[Category: Poulos, T L]]
[[Category: Poulos TL]]
[[Category: Tripathi, S M]]
[[Category: Tripathi SM]]
[[Category: Oxidoreductase-electron transport complex]]
[[Category: P450cam-pdx complex]]
[[Category: Redox partner]]

Latest revision as of 18:50, 20 September 2023

Crystal structure of Cytochrome P450cam-putidaredoxin complexCrystal structure of Cytochrome P450cam-putidaredoxin complex

Structural highlights

4jws is a 4 chain structure with sequence from Pseudomonas putida. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.15Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CPXA_PSEPU Involved in a camphor oxidation system.

Publication Abstract from PubMed

Cytochromes P450 catalyze a variety of monooxygenase reactions that require electron transfer from redox partners. Although the structure of many P450s and a small handful of redox partners are known, there is very little structural information available on redox complexes, thus leaving a gap in our understanding on the control of P450-redox partner interactions. We have solved the crystal structure of oxidized and reduced P450cam complexed with its redox partner, putidaredoxin (Pdx), to 2.2 and 2.09 angstroms, respectively. It was anticipated that Pdx would favor closed substrate-bound P450cam, which differs substantially from the open conformer, but instead we found that Pdx favors the open state. These new structures indicate that the effector role of Pdx is to shift P450cam toward the open conformation, which enables the establishment of a water-mediated H-bonded network, which is required for proton-coupled electron transfer.

Structural basis for effector control and redox partner recognition in cytochrome P450.,Tripathi S, Li H, Poulos TL Science. 2013 Jun 7;340(6137):1227-30. doi: 10.1126/science.1235797. PMID:23744947[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Tripathi S, Li H, Poulos TL. Structural basis for effector control and redox partner recognition in cytochrome P450. Science. 2013 Jun 7;340(6137):1227-30. doi: 10.1126/science.1235797. PMID:23744947 doi:10.1126/science.1235797

4jws, resolution 2.15Å

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