1ml2: Difference between revisions
No edit summary |
No edit summary |
||
Line 1: | Line 1: | ||
[[Image:1ml2.gif|left|200px]] | [[Image:1ml2.gif|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_1ml2", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
or leave the SCENE parameter empty for the default display. | |||
--> | |||
{{STRUCTURE_1ml2| PDB=1ml2 | SCENE= }} | |||
}} | |||
'''Crystal Structure of a Mutant Variant of Cytochrome c Peroxidase with Zn(II)-(20-oxo-Protoporphyrin IX)''' | '''Crystal Structure of a Mutant Variant of Cytochrome c Peroxidase with Zn(II)-(20-oxo-Protoporphyrin IX)''' | ||
Line 31: | Line 28: | ||
[[Category: Poulos, T L.]] | [[Category: Poulos, T L.]] | ||
[[Category: Shimizu, H.]] | [[Category: Shimizu, H.]] | ||
[[Category: | [[Category: Cytochrome c peroxidase]] | ||
[[Category: | [[Category: Oxygen radical]] | ||
[[Category: | [[Category: Trp cation radical]] | ||
[[Category: | [[Category: Trp-tyr covalent cross-link]] | ||
[[Category: | [[Category: Zn-protoporphyrin ix]] | ||
[[Category: | [[Category: Znccp]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:21:04 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on |
Revision as of 01:21, 3 May 2008
Crystal Structure of a Mutant Variant of Cytochrome c Peroxidase with Zn(II)-(20-oxo-Protoporphyrin IX)
OverviewOverview
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 StructureAbout this Structure
1ML2 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
ReferenceReference
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 Page seeded by OCA on Sat May 3 01:21:04 2008