1ebe
From Proteopedia
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|PDB= 1ebe |SIZE=350|CAPTION= <scene name='initialview01'>1ebe</scene>, resolution 2.2Å | |PDB= 1ebe |SIZE=350|CAPTION= <scene name='initialview01'>1ebe</scene>, resolution 2.2Å | ||
|SITE= <scene name='pdbsite=HEM:Hem+Binding+Site+For+Chain+A'>HEM</scene> and <scene name='pdbsite=OXO:Oxo+Binding+Site+For+Chain+A'>OXO</scene> | |SITE= <scene name='pdbsite=HEM:Hem+Binding+Site+For+Chain+A'>HEM</scene> and <scene name='pdbsite=OXO:Oxo+Binding+Site+For+Chain+A'>OXO</scene> | ||
| - | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> | + | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=O:OXYGEN+ATOM'>O</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= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ebe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ebe OCA], [http://www.ebi.ac.uk/pdbsum/1ebe PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ebe RCSB]</span> | ||
}} | }} | ||
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[[Category: Soltis, S M.]] | [[Category: Soltis, S M.]] | ||
[[Category: Wakatsuki, S.]] | [[Category: Wakatsuki, S.]] | ||
| - | [[Category: HEM]] | ||
| - | [[Category: O]] | ||
[[Category: compound i]] | [[Category: compound i]] | ||
[[Category: laue diffraction]] | [[Category: laue diffraction]] | ||
[[Category: oxidoreductase (h2o2(a))]] | [[Category: oxidoreductase (h2o2(a))]] | ||
| - | ''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 19:59:12 2008'' |
Revision as of 16:59, 30 March 2008
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| , resolution 2.2Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | and | ||||||
| Ligands: | , | ||||||
| Activity: | Cytochrome-c peroxidase, with EC number 1.11.1.5 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
LAUE DIFFRACTION STUDY ON THE STRUCTURE OF CYTOCHROME C PEROXIDASE COMPOUND I
Overview
BACKGROUND: Cytochrome c peroxidase from yeast is a soluble haem-containing protein found in the mitochondrial electron transport chain where it probably protects against toxic peroxides. The aim of this study was to obtain a reliable structure for the doubly oxidized transient intermediate (termed compound I) in the reaction of cytochrome c peroxidase with hydrogen peroxide. This intermediate contains a semistable free radical on Trp191, and an oxyferryl haem group. RESULTS: Compound I was produced in crystals of yeast cytochrome c peroxidase by reacting the crystalline enzyme with hydrogen peroxide in a flow cell. The reaction was monitored by microspectrophotometry and Laue crystallography in separate experiments. A nearly complete conversion to compound I was achieved within two minutes of the addition of hydrogen peroxide, and the concentration of the intermediate remained at similar levels for an additional half an hour. The structure of the intermediate was determined by Laue diffraction. The refined Laue structure for compound I shows clear structural changes at the peroxide-binding site but no significant changes at the radical site. The photographs were processed with a new software package (LEAP), overcoming many of the former problems encountered in extracting structural information from Laue exposures. CONCLUSIONS: The geometry of the haem environment in this protein allows structural changes to be extremely small, similar in magnitude to those observed for the Fe2+/Fe3+ transition in cytochrome c. The results suggest that these molecules have evolved to transfer electrons with a minimal need for structural adjustment.
About this Structure
1EBE is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Laue diffraction study on the structure of cytochrome c peroxidase compound I., Fulop V, Phizackerley RP, Soltis SM, Clifton IJ, Wakatsuki S, Erman J, Hajdu J, Edwards SL, Structure. 1994 Mar 15;2(3):201-8. PMID:8069633
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