1rf9: Difference between revisions
New page: left|200px<br /><applet load="1rf9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rf9, resolution 1.8Å" /> '''Crystal structure of ... |
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[[Image:1rf9.gif|left|200px]]<br /><applet load="1rf9" size=" | [[Image:1rf9.gif|left|200px]]<br /><applet load="1rf9" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1rf9, resolution 1.8Å" /> | caption="1rf9, resolution 1.8Å" /> | ||
'''Crystal structure of cytochrome P450-cam with a fluorescent probe D-4-AD (Adamantane-1-carboxylic acid-5-dimethylamino-naphthalene-1-sulfonylamino-butyl-amide)'''<br /> | '''Crystal structure of cytochrome P450-cam with a fluorescent probe D-4-AD (Adamantane-1-carboxylic acid-5-dimethylamino-naphthalene-1-sulfonylamino-butyl-amide)'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1RF9 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, DBR and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. 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:// | 1RF9 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=DBR:'>DBR</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1RF9 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: substrate-linked sensitizers]] | [[Category: substrate-linked sensitizers]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:42:14 2008'' | ||
Revision as of 15:42, 23 January 2008
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Crystal structure of cytochrome P450-cam with a fluorescent probe D-4-AD (Adamantane-1-carboxylic acid-5-dimethylamino-naphthalene-1-sulfonylamino-butyl-amide)
OverviewOverview
Members of the ubiquitous cytochrome P450 family catalyze a vast range of, biologically significant reactions in mammals, plants, fungi, and, bacteria. Some P450s display a remarkable promiscuity in substrate, recognition, while others are very specific with respect to substrate, binding or regio and stereo-selective catalysis. Recent results have, suggested that conformational flexibility in the substrate access channel, of many P450s may play an important role in controlling these effects., Here, we report the X-ray crystal structures at 1.8A and 1.5A of, cytochrome P450cam complexed with two synthetic molecular wires, D-4-Ad, and D-8-Ad, consisting of a dansyl fluorophore linked to an adamantyl, substrate analog via an alpha,omega-diaminoalkane chain of varying length., Both wires bind with the adamantyl moiety in similar positions at the, camphor-binding site. However, each wire induces a distinct conformational, response in the protein that differs from the camphor-bound structure. The, changes involve significant movements of the F, G, and I helices, allowing, the substrate access channel to adapt to the variable length of the probe., Wire-induced opening of the substrate channel also alters the I helix, bulge and Thr252 at the active site with binding of water that has been, proposed to assist in peroxy bond cleavage. The structures suggest that, the coupling of substrate-induced conformational changes to active-site, residues may be different in P450cam and recently described mammalian P450, structures. The wire-induced changes may be representative of the, conformational intermediates that must exist transiently during substrate, entry and product egress, providing a view of how substrates enter the, deeply buried active site. They also support observed examples of, conformational plasticity that are believed be responsible for the, promiscuity of drug metabolizing P450s. Observation of such large changes, in P450cam suggests that substrate channel plasticity is a general, property inherent to all P450 structures.
About this StructureAbout this Structure
1RF9 is a Single protein structure of sequence from Pseudomonas putida with , and as ligands. Active as Camphor 5-monooxygenase, with EC number 1.14.15.1 Full crystallographic information is available from OCA.
ReferenceReference
Conformational states of cytochrome P450cam revealed by trapping of synthetic molecular wires., Hays AM, Dunn AR, Chiu R, Gray HB, Stout CD, Goodin DB, J Mol Biol. 2004 Nov 19;344(2):455-69. PMID:15522298 [[Category: adamantane-1-carboxylic acid [4-(5-dimethylamino-naphthalene-1-sulfonylamino)-butyl]-amide]]
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