1fah: Difference between revisions

Revision as of 13:36, 21 February 2008

STRUCTURE OF CYTOCHROME P450

OverviewOverview

Cytochrome P450BM-3, a catalytically self-sufficient monooxygenase from Bacillus megaterium, catalyzes the omega-n (n = 1-3) hydroxylation of fatty acids in the presence of O2 and NADPH. Like most other P450s, cytochrome P450BM-3 contains a threonine residue (Thr268) in the distal I helix thought to be important for O2 binding and activation. Thr268 has been converted to alanine and the enzymatic properties and heme domain crystal structure determined. Using sodium laurate as the substrate, the mutant exhibited slower rates of O2 and NADPH consumption. In addition, electron transfer is uncoupled from substrate hydroxylation as evidenced by the greater production of water and peroxide in the mutant compared to the wild-type enzyme. The crystal structure of the mutant reveals that the only changes in structure are confined to the site of mutation. These data indicate an important role for Thr268 in O2 binding and activation in the metabolism of sodium laurate by cytochrome P450BM-3.

About this StructureAbout this Structure

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

ReferenceReference

The role of Thr268 in oxygen activation of cytochrome P450BM-3., Yeom H, Sligar SG, Li H, Poulos TL, Fulco AJ, Biochemistry. 1995 Nov 14;34(45):14733-40. PMID:7578081

Page seeded by OCA on Thu Feb 21 12:36:41 2008

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OCA

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-[[Image:1fah.jpg|left|200px]]<br /><applet load="1fah" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1fah.jpg|left|200px]]<br /><applet load="1fah" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1fah, resolution 2.3&Aring;" />
 '''STRUCTURE OF CYTOCHROME P450'''<br />
 ==Overview==
-Cytochrome P450BM-3, a catalytically self-sufficient monooxygenase from, Bacillus megaterium, catalyzes the omega-n (n = 1-3) hydroxylation of, fatty acids in the presence of O2 and NADPH. Like most other P450s, cytochrome P450BM-3 contains a threonine residue (Thr268) in the distal I, helix thought to be important for O2 binding and activation. Thr268 has, been converted to alanine and the enzymatic properties and heme domain, crystal structure determined. Using sodium laurate as the substrate, the, mutant exhibited slower rates of O2 and NADPH consumption. In addition, electron transfer is uncoupled from substrate hydroxylation as evidenced, by the greater production of water and peroxide in the mutant compared to, the wild-type enzyme. The crystal structure of the mutant reveals that the, only changes in structure are confined to the site of mutation. These data, indicate an important role for Thr268 in O2 binding and activation in the, metabolism of sodium laurate by cytochrome P450BM-3.
+Cytochrome P450BM-3, a catalytically self-sufficient monooxygenase from Bacillus megaterium, catalyzes the omega-n (n = 1-3) hydroxylation of fatty acids in the presence of O2 and NADPH. Like most other P450s, cytochrome P450BM-3 contains a threonine residue (Thr268) in the distal I helix thought to be important for O2 binding and activation. Thr268 has been converted to alanine and the enzymatic properties and heme domain crystal structure determined. Using sodium laurate as the substrate, the mutant exhibited slower rates of O2 and NADPH consumption. In addition, electron transfer is uncoupled from substrate hydroxylation as evidenced by the greater production of water and peroxide in the mutant compared to the wild-type enzyme. The crystal structure of the mutant reveals that the only changes in structure are confined to the site of mutation. These data indicate an important role for Thr268 in O2 binding and activation in the metabolism of sodium laurate by cytochrome P450BM-3.
 ==About this Structure==
-FAH 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 as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1FAH OCA].
+FAH 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> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1FAH OCA].
 ==Reference==
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 [[Category: Single protein]]
 [[Category: Unspecific monooxygenase]]
-[[Category: Li, H.Y.]]
+[[Category: Li, H Y.]]
-[[Category: Poulos, T.L.]]
+[[Category: Poulos, T L.]]
 [[Category: HEM]]
 [[Category: electron transport]]
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 [[Category: monooxygenase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:46:23 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:36:41 2008''