1izo
From Proteopedia
(New page: 200px<br /><applet load="1izo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1izo, resolution 2.10Å" /> '''Cytochrome P450 BS b...) |
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| - | [[Image:1izo.gif|left|200px]]<br /><applet load="1izo" size=" | + | [[Image:1izo.gif|left|200px]]<br /><applet load="1izo" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1izo, resolution 2.10Å" /> | caption="1izo, resolution 2.10Å" /> | ||
'''Cytochrome P450 BS beta Complexed with Fatty Acid'''<br /> | '''Cytochrome P450 BS beta Complexed with Fatty Acid'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Cytochrome P450 isolated from Bacillus subtilis (P450(BSbeta); molecular | + | Cytochrome P450 isolated from Bacillus subtilis (P450(BSbeta); molecular mass, 48 kDa) catalyzes the hydroxylation of a long-chain fatty acid (e.g. myristic acid) at the alpha- and beta-positions using hydrogen peroxide as an oxidant. We report here on the crystal structure of ferric P450(BSbeta) in the substrate-bound form, determined at a resolution of 2.1 A. P450(BSbeta) exhibits a typical P450 fold. The substrate binds to a specific channel in the enzyme and is stabilized through hydrophobic interactions of its alkyl side chain with some hydrophobic residues on the enzyme as well as by electrostatic interaction of its terminal carboxylate with the Arg(242) guanidium group. These interactions are responsible for the site specificity of the hydroxylation site in which the alpha- and beta-positions of the fatty acid come into close proximity to the heme iron sixth site. The fatty acid carboxylate group interacts with Arg(242) in the same fashion as has been reported for the active site of chloroperoxidase, His(105)-Glu(183), which is an acid-base catalyst in the peroxidation reactions. On the basis of these observations, a possible mechanism for the hydroxylation reaction catalyzed by P450(BSbeta) is proposed in which the carboxylate of the bound-substrate fatty acid assists in the cleavage of the peroxide O-O bond. |
==About this Structure== | ==About this Structure== | ||
| - | 1IZO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with HEM and PAM as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1IZO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=PAM:'>PAM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IZO OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Adachi, S.]] | [[Category: Adachi, S.]] | ||
[[Category: Ichihara, K.]] | [[Category: Ichihara, K.]] | ||
| - | [[Category: Lee, D | + | [[Category: Lee, D S.]] |
[[Category: Matsunaga, I.]] | [[Category: Matsunaga, I.]] | ||
[[Category: Ogura, H.]] | [[Category: Ogura, H.]] | ||
| - | [[Category: Park, S | + | [[Category: Park, S Y.]] |
| - | [[Category: RSGI, RIKEN | + | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] |
[[Category: Shiro, Y.]] | [[Category: Shiro, Y.]] | ||
[[Category: Sugimoto, H.]] | [[Category: Sugimoto, H.]] | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:17:26 2008'' |
Revision as of 11:17, 21 February 2008
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Cytochrome P450 BS beta Complexed with Fatty Acid
Overview
Cytochrome P450 isolated from Bacillus subtilis (P450(BSbeta); molecular mass, 48 kDa) catalyzes the hydroxylation of a long-chain fatty acid (e.g. myristic acid) at the alpha- and beta-positions using hydrogen peroxide as an oxidant. We report here on the crystal structure of ferric P450(BSbeta) in the substrate-bound form, determined at a resolution of 2.1 A. P450(BSbeta) exhibits a typical P450 fold. The substrate binds to a specific channel in the enzyme and is stabilized through hydrophobic interactions of its alkyl side chain with some hydrophobic residues on the enzyme as well as by electrostatic interaction of its terminal carboxylate with the Arg(242) guanidium group. These interactions are responsible for the site specificity of the hydroxylation site in which the alpha- and beta-positions of the fatty acid come into close proximity to the heme iron sixth site. The fatty acid carboxylate group interacts with Arg(242) in the same fashion as has been reported for the active site of chloroperoxidase, His(105)-Glu(183), which is an acid-base catalyst in the peroxidation reactions. On the basis of these observations, a possible mechanism for the hydroxylation reaction catalyzed by P450(BSbeta) is proposed in which the carboxylate of the bound-substrate fatty acid assists in the cleavage of the peroxide O-O bond.
About this Structure
1IZO is a Single protein structure of sequence from Bacillus subtilis with and as ligands. Full crystallographic information is available from OCA.
Reference
Substrate recognition and molecular mechanism of fatty acid hydroxylation by cytochrome P450 from Bacillus subtilis. Crystallographic, spectroscopic, and mutational studies., Lee DS, Yamada A, Sugimoto H, Matsunaga I, Ogura H, Ichihara K, Adachi S, Park SY, Shiro Y, J Biol Chem. 2003 Mar 14;278(11):9761-7. Epub 2003 Jan 7. PMID:12519760
Page seeded by OCA on Thu Feb 21 13:17:26 2008
Categories: Bacillus subtilis | Single protein | Adachi, S. | Ichihara, K. | Lee, D S. | Matsunaga, I. | Ogura, H. | Park, S Y. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Shiro, Y. | Sugimoto, H. | Yamada, A. | HEM | PAM | Heme protein | Protein-fatty acid complex | Riken structural genomics/proteomics initiative | Rsgi | Structural genomics
