1v8x
From Proteopedia
(New page: 200px<br /><applet load="1v8x" size="450" color="white" frame="true" align="right" spinBox="true" caption="1v8x, resolution 1.85Å" /> '''Crystal Structure of...) |
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| - | [[Image:1v8x.gif|left|200px]]<br /><applet load="1v8x" size=" | + | [[Image:1v8x.gif|left|200px]]<br /><applet load="1v8x" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1v8x, resolution 1.85Å" /> | caption="1v8x, resolution 1.85Å" /> | ||
'''Crystal Structure of the Dioxygen-bound Heme Oxygenase from Corynebacterium diphtheriae'''<br /> | '''Crystal Structure of the Dioxygen-bound Heme Oxygenase from Corynebacterium diphtheriae'''<br /> | ||
==Overview== | ==Overview== | ||
| - | HmuO, a heme oxygenase of Corynebacterium diphtheriae, catalyzes | + | HmuO, a heme oxygenase of Corynebacterium diphtheriae, catalyzes degradation of heme using the same mechanism as the mammalian enzyme. The oxy form of HmuO, the precursor of the catalytically active ferric hydroperoxo species, has been characterized by ligand binding kinetics, resonance Raman spectroscopy, and x-ray crystallography. The oxygen association and dissociation rate constants are 5 microm(-1) s(-1) and 0.22 s(-1), respectively, yielding an O(2) affinity of 21 microm(-1), which is approximately 20 times greater than that of mammalian myoglobins. However, the affinity of HmuO for CO is only 3-4-fold greater than that for mammalian myoglobins, implying the presence of strong hydrogen bonding interactions in the distal pocket of HmuO that preferentially favor O(2) binding. Resonance Raman spectra show that the Fe-O(2) vibrations are tightly coupled to porphyrin vibrations, indicating the highly bent Fe-O-O geometry that is characteristic of the oxy forms of heme oxygenases. In the crystal structure of the oxy form the Fe-O-O angle is 110 degrees, the O-O bond is pointed toward the heme alpha-meso-carbon by direct steric interactions with Gly-135 and Gly-139, and hydrogen bonds occur between the bound O(2) and the amide nitrogen of Gly-139 and a distal pocket water molecule, which is a part of an extended hydrogen bonding network that provides the solvent protons required for oxygen activation. In addition, the O-O bond is orthogonal to the plane of the proximal imidazole side chain, which facilitates hydroxylation of the porphyrin alpha-meso-carbon by preventing premature O-O bond cleavage. |
==About this Structure== | ==About this Structure== | ||
| - | 1V8X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Corynebacterium_diphtheriae Corynebacterium diphtheriae] with SUC, SO4, HEM and OXY as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Heme_oxygenase Heme oxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.3 1.14.99.3] Full crystallographic information is available from [http:// | + | 1V8X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Corynebacterium_diphtheriae Corynebacterium diphtheriae] with <scene name='pdbligand=SUC:'>SUC</scene>, <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=OXY:'>OXY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Heme_oxygenase Heme oxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.3 1.14.99.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V8X OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Heme oxygenase]] | [[Category: Heme oxygenase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Chu, G | + | [[Category: Chu, G C.]] |
[[Category: Couture, M.]] | [[Category: Couture, M.]] | ||
[[Category: Ikeda-Saito, M.]] | [[Category: Ikeda-Saito, M.]] | ||
[[Category: Matsui, T.]] | [[Category: Matsui, T.]] | ||
| - | [[Category: Olson, J | + | [[Category: Olson, J S.]] |
| - | [[Category: Rousseau, D | + | [[Category: Rousseau, D L.]] |
[[Category: Unno, M.]] | [[Category: Unno, M.]] | ||
[[Category: Yoshida, T.]] | [[Category: Yoshida, T.]] | ||
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[[Category: protein-heme complex]] | [[Category: protein-heme complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:32:45 2008'' |
Revision as of 13:32, 21 February 2008
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Crystal Structure of the Dioxygen-bound Heme Oxygenase from Corynebacterium diphtheriae
Overview
HmuO, a heme oxygenase of Corynebacterium diphtheriae, catalyzes degradation of heme using the same mechanism as the mammalian enzyme. The oxy form of HmuO, the precursor of the catalytically active ferric hydroperoxo species, has been characterized by ligand binding kinetics, resonance Raman spectroscopy, and x-ray crystallography. The oxygen association and dissociation rate constants are 5 microm(-1) s(-1) and 0.22 s(-1), respectively, yielding an O(2) affinity of 21 microm(-1), which is approximately 20 times greater than that of mammalian myoglobins. However, the affinity of HmuO for CO is only 3-4-fold greater than that for mammalian myoglobins, implying the presence of strong hydrogen bonding interactions in the distal pocket of HmuO that preferentially favor O(2) binding. Resonance Raman spectra show that the Fe-O(2) vibrations are tightly coupled to porphyrin vibrations, indicating the highly bent Fe-O-O geometry that is characteristic of the oxy forms of heme oxygenases. In the crystal structure of the oxy form the Fe-O-O angle is 110 degrees, the O-O bond is pointed toward the heme alpha-meso-carbon by direct steric interactions with Gly-135 and Gly-139, and hydrogen bonds occur between the bound O(2) and the amide nitrogen of Gly-139 and a distal pocket water molecule, which is a part of an extended hydrogen bonding network that provides the solvent protons required for oxygen activation. In addition, the O-O bond is orthogonal to the plane of the proximal imidazole side chain, which facilitates hydroxylation of the porphyrin alpha-meso-carbon by preventing premature O-O bond cleavage.
About this Structure
1V8X is a Single protein structure of sequence from Corynebacterium diphtheriae with , , and as ligands. Active as Heme oxygenase, with EC number 1.14.99.3 Full crystallographic information is available from OCA.
Reference
Crystal structure of the dioxygen-bound heme oxygenase from Corynebacterium diphtheriae: implications for heme oxygenase function., Unno M, Matsui T, Chu GC, Couture M, Yoshida T, Rousseau DL, Olson JS, Ikeda-Saito M, J Biol Chem. 2004 May 14;279(20):21055-61. Epub 2004 Feb 13. PMID:14966119
Page seeded by OCA on Thu Feb 21 15:32:45 2008
Categories: Corynebacterium diphtheriae | Heme oxygenase | Single protein | Chu, G C. | Couture, M. | Ikeda-Saito, M. | Matsui, T. | Olson, J S. | Rousseau, D L. | Unno, M. | Yoshida, T. | HEM | OXY | SO4 | SUC | Helix | Oxy | Protein-heme complex
