3cpp: Difference between revisions
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New page: left|200px<br /> <applet load="3cpp" size="450" color="white" frame="true" align="right" spinBox="true" caption="3cpp, resolution 1.9Å" /> '''CRYSTAL STRUCTURE OF... |
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[[Image:3cpp.gif|left|200px]]<br /> | [[Image:3cpp.gif|left|200px]]<br /><applet load="3cpp" size="350" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="3cpp" size=" | |||
caption="3cpp, resolution 1.9Å" /> | caption="3cpp, resolution 1.9Å" /> | ||
'''CRYSTAL STRUCTURE OF THE CARBON MONOXY-SUBSTRATE-CYTOCHROME P450-CAM TERNARY COMPLEX'''<br /> | '''CRYSTAL STRUCTURE OF THE CARBON MONOXY-SUBSTRATE-CYTOCHROME P450-CAM TERNARY COMPLEX'''<br /> | ||
==Overview== | ==Overview== | ||
The crystal structure of the ternary complex formed between carbon | 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. | ||
==About this Structure== | ==About this Structure== | ||
3CPP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida] with HEM, CMO and CAM as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 3CPP with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb82_1.html Cytochrome p450]]. Active as [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] Full crystallographic information is available from [http:// | 3CPP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida] with <scene name='pdbligand=HEM:'>HEM</scene>, <scene name='pdbligand=CMO:'>CMO</scene> and <scene name='pdbligand=CAM:'>CAM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 3CPP with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb82_1.html Cytochrome p450]]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CPP OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Pseudomonas putida]] | [[Category: Pseudomonas putida]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Poulos, T | [[Category: Poulos, T L.]] | ||
[[Category: Raag, R.]] | [[Category: Raag, R.]] | ||
[[Category: CAM]] | [[Category: CAM]] | ||
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[[Category: oxidoreductase(oxygenase)]] | [[Category: oxidoreductase(oxygenase)]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:08:51 2008'' | ||