6atj
From Proteopedia
(New page: 200px<br /><applet load="6atj" size="450" color="white" frame="true" align="right" spinBox="true" caption="6atj, resolution 2.00Å" /> '''RECOMBINANT HORSERAD...) |
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| - | [[Image:6atj.gif|left|200px]]<br /><applet load="6atj" size=" | + | [[Image:6atj.gif|left|200px]]<br /><applet load="6atj" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="6atj, resolution 2.00Å" /> | caption="6atj, resolution 2.00Å" /> | ||
'''RECOMBINANT HORSERADISH PEROXIDASE C COMPLEX WITH FERULIC ACID'''<br /> | '''RECOMBINANT HORSERADISH PEROXIDASE C COMPLEX WITH FERULIC ACID'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We have solved the x-ray structures of the binary horseradish peroxidase | + | We have solved the x-ray structures of the binary horseradish peroxidase C-ferulic acid complex and the ternary horseradish peroxidase C-cyanide-ferulic acid complex to 2.0 and 1.45 A, respectively. Ferulic acid is a naturally occurring phenolic compound found in the plant cell wall and is an in vivo substrate for plant peroxidases. The x-ray structures demonstrate the flexibility and dynamic character of the aromatic donor binding site in horseradish peroxidase and emphasize the role of the distal arginine (Arg(38)) in both substrate oxidation and ligand binding. Arg(38) hydrogen bonds to bound cyanide, thereby contributing to the stabilization of the horseradish peroxidase-cyanide complex and suggesting that the distal arginine will be able to contribute with a similar interaction during stabilization of a bound peroxy transition state and subsequent O-O bond cleavage. The catalytic arginine is additionally engaged in an extensive hydrogen bonding network, which also includes the catalytic distal histidine, a water molecule and Pro(139), a proline residue conserved within the plant peroxidase superfamily. Based on the observed hydrogen bonding network and previous spectroscopic and kinetic work, a general mechanism of peroxidase substrate oxidation is proposed. |
==About this Structure== | ==About this Structure== | ||
| - | 6ATJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Armoracia_rusticana Armoracia rusticana] with CA, HEM and FER as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Peroxidase Peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.7 1.11.1.7] Full crystallographic information is available from [http:// | + | 6ATJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Armoracia_rusticana Armoracia rusticana] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=FER:'>FER</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Peroxidase Peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.7 1.11.1.7] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ATJ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Gajhede, M.]] | [[Category: Gajhede, M.]] | ||
[[Category: Henriksen, A.]] | [[Category: Henriksen, A.]] | ||
| - | [[Category: Smith, A | + | [[Category: Smith, A T.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: FER]] | [[Category: FER]] | ||
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[[Category: reducing substrate]] | [[Category: reducing substrate]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:16:05 2008'' |
Revision as of 17:16, 21 February 2008
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RECOMBINANT HORSERADISH PEROXIDASE C COMPLEX WITH FERULIC ACID
Overview
We have solved the x-ray structures of the binary horseradish peroxidase C-ferulic acid complex and the ternary horseradish peroxidase C-cyanide-ferulic acid complex to 2.0 and 1.45 A, respectively. Ferulic acid is a naturally occurring phenolic compound found in the plant cell wall and is an in vivo substrate for plant peroxidases. The x-ray structures demonstrate the flexibility and dynamic character of the aromatic donor binding site in horseradish peroxidase and emphasize the role of the distal arginine (Arg(38)) in both substrate oxidation and ligand binding. Arg(38) hydrogen bonds to bound cyanide, thereby contributing to the stabilization of the horseradish peroxidase-cyanide complex and suggesting that the distal arginine will be able to contribute with a similar interaction during stabilization of a bound peroxy transition state and subsequent O-O bond cleavage. The catalytic arginine is additionally engaged in an extensive hydrogen bonding network, which also includes the catalytic distal histidine, a water molecule and Pro(139), a proline residue conserved within the plant peroxidase superfamily. Based on the observed hydrogen bonding network and previous spectroscopic and kinetic work, a general mechanism of peroxidase substrate oxidation is proposed.
About this Structure
6ATJ is a Single protein structure of sequence from Armoracia rusticana with , and as ligands. Active as Peroxidase, with EC number 1.11.1.7 Full crystallographic information is available from OCA.
Reference
The structures of the horseradish peroxidase C-ferulic acid complex and the ternary complex with cyanide suggest how peroxidases oxidize small phenolic substrates., Henriksen A, Smith AT, Gajhede M, J Biol Chem. 1999 Dec 3;274(49):35005-11. PMID:10574977
Page seeded by OCA on Thu Feb 21 19:16:05 2008
Categories: Armoracia rusticana | Peroxidase | Single protein | Gajhede, M. | Henriksen, A. | Smith, A T. | CA | FER | HEM | Oxidoreductase | Reducing substrate
