3cpp

<StructureSection load='3cpp' size='340' side='right' caption='[[3cpp]], [[Resolution|resolution]] 1.90&Aring;' scene=''>

<table><tr><td colspan='2'>[[3cpp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. The October 2006 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Cytochrome p450'' by David S. Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2006_10 10.2210/rcsb_pdb/mom_2006_10]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CPP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3CPP FirstGlance]. <br>

</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAM:CAMPHOR'>CAM</scene>, <scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene><br>

<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=3cpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cpp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3cpp RCSB], [http://www.ebi.ac.uk/pdbsum/3cpp PDBsum]</span></td></tr>

<table>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cp/3cpp_consurf.spt"</scriptWhenChecked>

</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].

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== Publication Abstract from PubMed ==

The crystal structure of the ternary complex formed between carbon monoxide (CO), camphor, and ferrous cytochrome P-450CAM has been refined to an R value of 17.9% at 1.9-A resolution. To accommodate the CO molecule, the substrate, camphor, moves about 0.8 A while at the same time remaining in nonbonded contact with CO. The average temperature factor of the camphor atoms is about 50% higher in the CO complex, suggesting that the camphor is more loosely bound in this ternary complex. The Fe-C-O angle is about 166 degrees, and thus, CO appears to be bent from the heme normal, as it is in various CO-globin complexes, due to steric interactions with active site groups. The oxygen atom of the CO molecule is nestled into a groove formed by an unusual helical hydrogen bond in the distal helix between the highly conserved Thr 252 and Gly 248 residues. In the transition from the ferric camphor-bound binary complex to the ferrous CO-camphor-bound ternary complex, the heme iron atom moves into the plane defined by the pyrrole nitrogens by about 0.41 A. Although the axial Cys ligand also moves toward the heme, the S-Fe bond stretches from about 2.20 A in the absence of CO to about 2.41 A once CO has bound.

Crystal structure of the carbon monoxide-substrate-cytochrome P-450CAM ternary complex.,Raag R, Poulos TL Biochemistry. 1989 Sep 19;28(19):7586-92. PMID:2611203<ref>PMID:2611203</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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*[[Cytochrome P450|Cytochrome P450]]

[[Category: Camphor 5-monooxygenase]]

[[Category: Poulos, T L.]]

[[Category: Raag, R.]]