1ml2
From Proteopedia
(New page: 200px<br /><applet load="1ml2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ml2, resolution 1.65Å" /> '''Crystal Structure of...) |
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| - | [[Image:1ml2.gif|left|200px]]<br /><applet load="1ml2" size=" | + | [[Image:1ml2.gif|left|200px]]<br /><applet load="1ml2" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ml2, resolution 1.65Å" /> | caption="1ml2, resolution 1.65Å" /> | ||
'''Crystal Structure of a Mutant Variant of Cytochrome c Peroxidase with Zn(II)-(20-oxo-Protoporphyrin IX)'''<br /> | '''Crystal Structure of a Mutant Variant of Cytochrome c Peroxidase with Zn(II)-(20-oxo-Protoporphyrin IX)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of a cytochrome c peroxidase mutant where the distal | + | The crystal structure of a cytochrome c peroxidase mutant where the distal catalytic His52 is converted to Tyr reveals that the tyrosine side-chain forms a covalent bond with the indole ring nitrogen atom of Trp51. We hypothesize that this novel bond results from peroxide activation by the heme iron followed by oxidation of Trp51 and Tyr52. This hypothesis has been tested by incorporation of a redox-inactive Zn-protoporphyrin into the protein, and the resulting crystal structure shows the absence of a Trp51-Tyr52 cross-link. Instead, the Tyr52 side-chain orients away from the heme active-site pocket, which requires a substantial rearrangement of residues 72-80 and 134-144. Additional experiments where heme-containing crystals of the mutant were treated with peroxide support our hypothesis that this novel Trp-Tyr cross-link is a peroxide-dependent process mediated by the heme iron. |
==About this Structure== | ==About this Structure== | ||
| - | 1ML2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with ZEM as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Cytochrome-c_peroxidase Cytochrome-c peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.5 1.11.1.5] Full crystallographic information is available from [http:// | + | 1ML2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=ZEM:'>ZEM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Cytochrome-c_peroxidase Cytochrome-c peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.5 1.11.1.5] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ML2 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bhaskar, B.]] | [[Category: Bhaskar, B.]] | ||
| - | [[Category: Farmer, P | + | [[Category: Farmer, P J.]] |
| - | [[Category: Immoos, C | + | [[Category: Immoos, C E.]] |
| - | [[Category: Poulos, T | + | [[Category: Poulos, T L.]] |
[[Category: Shimizu, H.]] | [[Category: Shimizu, H.]] | ||
[[Category: ZEM]] | [[Category: ZEM]] | ||
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[[Category: znccp]] | [[Category: znccp]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:56:16 2008'' |
Revision as of 11:56, 21 February 2008
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Crystal Structure of a Mutant Variant of Cytochrome c Peroxidase with Zn(II)-(20-oxo-Protoporphyrin IX)
Overview
The crystal structure of a cytochrome c peroxidase mutant where the distal catalytic His52 is converted to Tyr reveals that the tyrosine side-chain forms a covalent bond with the indole ring nitrogen atom of Trp51. We hypothesize that this novel bond results from peroxide activation by the heme iron followed by oxidation of Trp51 and Tyr52. This hypothesis has been tested by incorporation of a redox-inactive Zn-protoporphyrin into the protein, and the resulting crystal structure shows the absence of a Trp51-Tyr52 cross-link. Instead, the Tyr52 side-chain orients away from the heme active-site pocket, which requires a substantial rearrangement of residues 72-80 and 134-144. Additional experiments where heme-containing crystals of the mutant were treated with peroxide support our hypothesis that this novel Trp-Tyr cross-link is a peroxide-dependent process mediated by the heme iron.
About this Structure
1ML2 is a Single protein structure of sequence from Saccharomyces cerevisiae with as ligand. Active as Cytochrome-c peroxidase, with EC number 1.11.1.5 Full crystallographic information is available from OCA.
Reference
A novel heme and peroxide-dependent tryptophan-tyrosine cross-link in a mutant of cytochrome c peroxidase., Bhaskar B, Immoos CE, Shimizu H, Sulc F, Farmer PJ, Poulos TL, J Mol Biol. 2003 Apr 18;328(1):157-66. PMID:12684005
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