2feu: Difference between revisions

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==P450CAM from Pseudomonas putida reconstituted with manganic protoporphyrin IX==
==P450CAM from Pseudomonas putida reconstituted with manganic protoporphyrin IX==
<StructureSection load='2feu' size='340' side='right' caption='[[2feu]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='2feu' size='340' side='right' caption='[[2feu]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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<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='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='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=2feu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2feu OCA], [http://pdbe.org/2feu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2feu RCSB], [http://www.ebi.ac.uk/pdbsum/2feu PDBsum]</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=2feu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2feu OCA], [http://pdbe.org/2feu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2feu RCSB], [http://www.ebi.ac.uk/pdbsum/2feu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2feu ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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</div>
</div>
<div class="pdbe-citations 2feu" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 2feu" style="background-color:#fffaf0;"></div>
==See Also==
*[[Cytochrome P450|Cytochrome P450]]
== References ==
== References ==
<references/>
<references/>

Revision as of 10:37, 18 October 2017

P450CAM from Pseudomonas putida reconstituted with manganic protoporphyrin IXP450CAM from Pseudomonas putida reconstituted with manganic protoporphyrin IX

Structural highlights

2feu is a 2 chain structure with sequence from "bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , ,
Gene:camC, cyp101 ("Bacillus fluorescens putidus" Flugge 1886)
Activity:Camphor 5-monooxygenase, with EC number 1.14.15.1
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CPXA_PSEPU] Involved in a camphor oxidation system.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The oxidative prowess of the P450 cytochromes in physiological reactions is attributed to the production of a high-valent iron-oxo complex, or Compound I intermediate, in the reaction cycle. Despite many years of study, however, the full electronic description of this fleeting intermediate still remains an active area of study. In this manuscript, the current status of the isolation and characterization of the P450 oxo-Fe(IV) is examined and compared to analogous states in related heme enzymes. In addition, the utilization of cofactor exchange to stabilize high-valent oxo-states in the P450 is addressed. Structural and spectroscopic studies on manganese reconstituted P450, and its corresponding oxo-complex, are presented.

The status of high-valent metal oxo complexes in the P450 cytochromes.,Makris TM, von Koenig K, Schlichting I, Sligar SG J Inorg Biochem. 2006 Apr;100(4):507-18. Epub 2006 Feb 28. PMID:16510191[1]

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

References

  1. Makris TM, von Koenig K, Schlichting I, Sligar SG. The status of high-valent metal oxo complexes in the P450 cytochromes. J Inorg Biochem. 2006 Apr;100(4):507-18. Epub 2006 Feb 28. PMID:16510191 doi:http://dx.doi.org/10.1016/j.jinorgbio.2006.01.025

2feu, resolution 1.70Å

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