1ebe | pdb_00001ebe

Laue diffraction study on the structure of cytochrome c peroxidase compound I

spinqualitylabelsall models 1ebe, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ebe is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: HEM, O Related: 1a2f, 1a2g, 1aa4, 1ac4, 1ac8, 1aeb, 1aed, 1aee, 1aef, 1aeg, 1aeh, 1aej, 1aek, 1aem, 1aen, 1aeo, 1aeq, 1aes, 1aet, 1aeu, 1aev, 1bej, 1bek, 1bem, 1bep, 1beq, 1bes, 1bj9, 1bva, 1cca, 1ccb, 1ccc, 1cce, 1ccg, 1cci, 1ccj, 1cck, 1ccl, 1ccp, 1cmp, 1cmq, 1cmt, 1cmu, 1cpd, 1cpe, 1cpf, 1cpg, 1cyf, 1dcc, 1dj1, 1dj5, 1ds4, 1dse, 1dsg, 1dso, 1dsp, 1jdr, 1ryc, 2ccp, 2cyp, 2pcb, 2pcc, 3ccp, 3ccx, 4ccp, 4ccx, 5ccp, 6ccp, 7ccp Activity: Cytochrome-c peroxidase, with EC number 1.11.1.5 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CCPR_YEAST] Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cytochrome c peroxidase 3D structures

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