1ml2
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1ml2 |SIZE=350|CAPTION= <scene name='initialview01'>1ml2</scene>, resolution 1.65Å | |PDB= 1ml2 |SIZE=350|CAPTION= <scene name='initialview01'>1ml2</scene>, resolution 1.65Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ZEM:20-OXO-PROTOPORPHYRIN IX CONTAINING ZN(II)'>ZEM</scene> | + | |LIGAND= <scene name='pdbligand=ZEM:20-OXO-PROTOPORPHYRIN+IX+CONTAINING+ZN(II)'>ZEM</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= OPBYC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | |GENE= OPBYC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1mk8|1MK8]], [[1mkq|1MKQ]], [[1mkr|1MKR]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ml2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ml2 OCA], [http://www.ebi.ac.uk/pdbsum/1ml2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ml2 RCSB]</span> | ||
}} | }} | ||
| Line 28: | Line 31: | ||
[[Category: Poulos, T L.]] | [[Category: Poulos, T L.]] | ||
[[Category: Shimizu, H.]] | [[Category: Shimizu, H.]] | ||
| - | [[Category: ZEM]] | ||
[[Category: cytochrome c peroxidase]] | [[Category: cytochrome c peroxidase]] | ||
[[Category: oxygen radical]] | [[Category: oxygen radical]] | ||
| Line 36: | Line 38: | ||
[[Category: znccp]] | [[Category: znccp]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:17:30 2008'' |
Revision as of 19:17, 30 March 2008
| |||||||
| , resolution 1.65Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | OPBYC (Saccharomyces cerevisiae) | ||||||
| Activity: | Cytochrome-c peroxidase, with EC number 1.11.1.5 | ||||||
| Related: | 1MK8, 1MKQ, 1MKR
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
Page seeded by OCA on Sun Mar 30 22:17:30 2008
