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[[Image: | ==Optical detection of cytochrome P450 by sensitizer-linked substrates== | ||
<StructureSection load='1qmq' size='340' side='right' caption='[[1qmq]], [[Resolution|resolution]] 1.55Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1qmq]] is a 1 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=1QMQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QMQ FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=DRB:DELTA-BIS(2,2-BIPYRIDINE)-(5-METHYL-2-2-BIPYRIDINE)-C9-ADAMANTANE+RUTHENIUM+(II)'>DRB</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=LRB:LAMBDA-BIS(2,2-BIPYRIDINE)-(5-METHYL-2-2-BIPYRIDINE)-C9-ADAMANTANE+RUTHENIUM+(II)'>LRB</scene><br> | |||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1dz9|1dz9]], [[5cp4|5cp4]], [[1pha|1pha]], [[2h7q|2h7q]], [[1dz6|1dz6]], [[1t88|1t88]], [[2cpp|2cpp]], [[1p2y|1p2y]], [[6cpp|6cpp]], [[5cpp|5cpp]], [[1iwk|1iwk]], [[4cp4|4cp4]], [[2a1m|2a1m]], [[1j51|1j51]], [[1geb|1geb]], [[2fe6|2fe6]], [[1rf9|1rf9]], [[1t87|1t87]], [[1akd|1akd]], [[2h7r|2h7r]], [[1dz4|1dz4]], [[8cpp|8cpp]], [[1cp4|1cp4]], [[4cpp|4cpp]], [[1phc|1phc]], [[1o76|1o76]], [[2h7s|2h7s]], [[1phb|1phb]], [[1iwi|1iwi]], [[6cp4|6cp4]], [[1c8j|1c8j]], [[1phd|1phd]], [[1phg|1phg]], [[1noo|1noo]], [[1uyu|1uyu]], [[7cpp|7cpp]], [[1gjm|1gjm]], [[1dz8|1dz8]], [[2feu|2feu]], [[1t86|1t86]], [[2cp4|2cp4]], [[1t85|1t85]], [[1lwl|1lwl]], [[1phf|1phf]], [[1yrd|1yrd]], [[1k2o|1k2o]], [[1gek|1gek]], [[3cpp|3cpp]], [[1re9|1re9]], [[1phe|1phe]], [[2a1o|2a1o]], [[2a1n|2a1n]], [[2fer|2fer]], [[1p7r|1p7r]], [[1iwj|1iwj]], [[1gem|1gem]], [[3cp4|3cp4]], [[1yrc|1yrc]], [[1mpw|1mpw]]</td></tr> | |||
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CYP101 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=303 Pseudomonas putida])</td></tr> | |||
<tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qmq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qmq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1qmq RCSB], [http://www.ebi.ac.uk/pdbsum/1qmq PDBsum]</span></td></tr> | |||
<table> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qm/1qmq_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The ability to detect, characterize, and manipulate specific biomolecules in complex media is critical for understanding metabolic processes. Particularly important targets are oxygenases (cytochromes P450) involved in drug metabolism and many disease states, including liver and kidney dysfunction, neurological disorders, and cancer. We have found that Ru photosensitizers linked to P450 substrates specifically recognize submicromolar cytochrome P450(cam) in the presence of other heme proteins. In the P450:Ru-substrate conjugates, energy transfer to the heme dramatically accelerates the Ru-luminescence decay. The crystal structure of a P450(cam):Ru-adamantyl complex reveals access to the active center via a channel whose depth (Ru-Fe distance is 21 A) is virtually the same as that extracted from an analysis of the energy-transfer kinetics. Suitably constructed libraries of sensitizer-linked substrates could be employed to probe the steric and electronic properties of buried active sites. | |||
Optical detection of cytochrome P450 by sensitizer-linked substrates.,Dmochowski IJ, Crane BR, Wilker JJ, Winkler JR, Gray HB Proc Natl Acad Sci U S A. 1999 Nov 9;96(23):12987-90. PMID:10557259<ref>PMID:10557259</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Cytochrome P450|Cytochrome P450]] | *[[Cytochrome P450|Cytochrome P450]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Camphor 5-monooxygenase]] | [[Category: Camphor 5-monooxygenase]] | ||
[[Category: Pseudomonas putida]] | [[Category: Pseudomonas putida]] | ||
Revision as of 00:08, 29 September 2014
Optical detection of cytochrome P450 by sensitizer-linked substratesOptical detection of cytochrome P450 by sensitizer-linked substrates
Structural highlights
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 PubMedThe ability to detect, characterize, and manipulate specific biomolecules in complex media is critical for understanding metabolic processes. Particularly important targets are oxygenases (cytochromes P450) involved in drug metabolism and many disease states, including liver and kidney dysfunction, neurological disorders, and cancer. We have found that Ru photosensitizers linked to P450 substrates specifically recognize submicromolar cytochrome P450(cam) in the presence of other heme proteins. In the P450:Ru-substrate conjugates, energy transfer to the heme dramatically accelerates the Ru-luminescence decay. The crystal structure of a P450(cam):Ru-adamantyl complex reveals access to the active center via a channel whose depth (Ru-Fe distance is 21 A) is virtually the same as that extracted from an analysis of the energy-transfer kinetics. Suitably constructed libraries of sensitizer-linked substrates could be employed to probe the steric and electronic properties of buried active sites. Optical detection of cytochrome P450 by sensitizer-linked substrates.,Dmochowski IJ, Crane BR, Wilker JJ, Winkler JR, Gray HB Proc Natl Acad Sci U S A. 1999 Nov 9;96(23):12987-90. PMID:10557259[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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