1fag

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(New page: 200px<br /><applet load="1fag" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fag, resolution 2.7&Aring;" /> '''STRUCTURE OF CYTOCHRO...)
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[[Image:1fag.gif|left|200px]]<br /><applet load="1fag" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1fag.gif|left|200px]]<br /><applet load="1fag" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1fag, resolution 2.7&Aring;" />
caption="1fag, resolution 2.7&Aring;" />
'''STRUCTURE OF CYTOCHROME P450'''<br />
'''STRUCTURE OF CYTOCHROME P450'''<br />
==Overview==
==Overview==
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The substrate-bound structures of two cytochrome P450s, P450cam and, P450eryF, are known. While these structures reveal important features that, control substrate specificity, the problem of how conformational changes, allow for substrate entry and product release remains unsolved. The, structure of the haem domain of the bacterial fatty acid hydroxylase, P450BM-3, previously was solved in the substrate-free form. Unlike the, substrate-bound P450cam and P450eryF structures, the substrate access, channel is open in substrate-free P450BM-3. Here we present the X-ray, structure of P450BM-3 at 2.7 A bound with a fatty acid substrate, palmitoleic acid. A comparison of the substrate-bound and -free forms, reveals major conformational differences and provides the first detailed, picture of substrate-induced conformational changes in a P450.
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The substrate-bound structures of two cytochrome P450s, P450cam and P450eryF, are known. While these structures reveal important features that control substrate specificity, the problem of how conformational changes allow for substrate entry and product release remains unsolved. The structure of the haem domain of the bacterial fatty acid hydroxylase, P450BM-3, previously was solved in the substrate-free form. Unlike the substrate-bound P450cam and P450eryF structures, the substrate access channel is open in substrate-free P450BM-3. Here we present the X-ray structure of P450BM-3 at 2.7 A bound with a fatty acid substrate, palmitoleic acid. A comparison of the substrate-bound and -free forms reveals major conformational differences and provides the first detailed picture of substrate-induced conformational changes in a P450.
==About this Structure==
==About this Structure==
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1FAG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_megaterium Bacillus megaterium] with HEM and PAM as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Unspecific_monooxygenase Unspecific monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.14.1 1.14.14.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FAG OCA].
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1FAG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_megaterium Bacillus megaterium] with <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=PAM:'>PAM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Unspecific_monooxygenase Unspecific monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.14.1 1.14.14.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FAG OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Unspecific monooxygenase]]
[[Category: Unspecific monooxygenase]]
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[[Category: Li, H.Y.]]
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[[Category: Li, H Y.]]
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[[Category: Poulos, T.L.]]
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[[Category: Poulos, T L.]]
[[Category: HEM]]
[[Category: HEM]]
[[Category: PAM]]
[[Category: PAM]]
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[[Category: monooxygenase]]
[[Category: monooxygenase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:46:19 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:36:36 2008''

Revision as of 10:36, 21 February 2008


1fag, resolution 2.7Å

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STRUCTURE OF CYTOCHROME P450

Overview

The substrate-bound structures of two cytochrome P450s, P450cam and P450eryF, are known. While these structures reveal important features that control substrate specificity, the problem of how conformational changes allow for substrate entry and product release remains unsolved. The structure of the haem domain of the bacterial fatty acid hydroxylase, P450BM-3, previously was solved in the substrate-free form. Unlike the substrate-bound P450cam and P450eryF structures, the substrate access channel is open in substrate-free P450BM-3. Here we present the X-ray structure of P450BM-3 at 2.7 A bound with a fatty acid substrate, palmitoleic acid. A comparison of the substrate-bound and -free forms reveals major conformational differences and provides the first detailed picture of substrate-induced conformational changes in a P450.

About this Structure

1FAG is a Single protein structure of sequence from Bacillus megaterium with and as ligands. Active as Unspecific monooxygenase, with EC number 1.14.14.1 Full crystallographic information is available from OCA.

Reference

The structure of the cytochrome p450BM-3 haem domain complexed with the fatty acid substrate, palmitoleic acid., Li H, Poulos TL, Nat Struct Biol. 1997 Feb;4(2):140-6. PMID:9033595

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