1ebe

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Revision as of 05:46, 10 September 2015

LAUE DIFFRACTION STUDY ON THE STRUCTURE OF CYTOCHROME C PEROXIDASE COMPOUND I

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:	,
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

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Fulop V, Phizackerley RP, Soltis SM, Clifton IJ, Wakatsuki S, Erman J, Hajdu J, Edwards SL. Laue diffraction study on the structure of cytochrome c peroxidase compound I. Structure. 1994 Mar 15;2(3):201-8. PMID:8069633

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ebe"

@@ Line 6: / Line 6: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1a2f|1a2f]], [[1a2g|1a2g]], [[1aa4|1aa4]], [[1ac4|1ac4]], [[1ac8|1ac8]], [[1aeb|1aeb]], [[1aed|1aed]], [[1aee|1aee]], [[1aef|1aef]], [[1aeg|1aeg]], [[1aeh|1aeh]], [[1aej|1aej]], [[1aek|1aek]], [[1aem|1aem]], [[1aen|1aen]], [[1aeo|1aeo]], [[1aeq|1aeq]], [[1aes|1aes]], [[1aet|1aet]], [[1aeu|1aeu]], [[1aev|1aev]], [[1bej|1bej]], [[1bek|1bek]], [[1bem|1bem]], [[1bep|1bep]], [[1beq|1beq]], [[1bes|1bes]], [[1bj9|1bj9]], [[1bva|1bva]], [[1cca|1cca]], [[1ccb|1ccb]], [[1ccc|1ccc]], [[1cce|1cce]], [[1ccg|1ccg]], [[1cci|1cci]], [[1ccj|1ccj]], [[1cck|1cck]], [[1ccl|1ccl]], [[1ccp|1ccp]], [[1cmp|1cmp]], [[1cmq|1cmq]], [[1cmt|1cmt]], [[1cmu|1cmu]], [[1cpd|1cpd]], [[1cpe|1cpe]], [[1cpf|1cpf]], [[1cpg|1cpg]], [[1cyf|1cyf]], [[1dcc|1dcc]], [[1dj1|1dj1]], [[1dj5|1dj5]], [[1ds4|1ds4]], [[1dse|1dse]], [[1dsg|1dsg]], [[1dso|1dso]], [[1dsp|1dsp]], [[1jdr|1jdr]], [[1ryc|1ryc]], [[2ccp|2ccp]], [[2cyp|2cyp]], [[2pcb|2pcb]], [[2pcc|2pcc]], [[3ccp|3ccp]], [[3ccx|3ccx]], [[4ccp|4ccp]], [[4ccx|4ccx]], [[5ccp|5ccp]], [[6ccp|6ccp]], [[7ccp|7ccp]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1ebe RCSB], [http://www.ebi.ac.uk/pdbsum/1ebe PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1ebe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ebe RCSB], [http://www.ebi.ac.uk/pdbsum/1ebe PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 28: / Line 28: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1ebe" style="background-color:#fffaf0;"></div>
 ==See Also==

1ebe

From Proteopedia

Revision as of 05:46, 10 September 2015

LAUE DIFFRACTION STUDY ON THE STRUCTURE OF CYTOCHROME C PEROXIDASE COMPOUND I

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

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