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1eb7

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[[Image:1eb7.jpg|left|200px]]<br /><applet load="1eb7" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1eb7, resolution 2.4&Aring;" />
 
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'''CRYSTAL STRUCTURE OF THE DI-HAEM CYTOCHROME C PEROXIDASE FROM PSEUDOMONAS AERUGINOSA'''<br />
 
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==Overview==
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==Crystal structure of the di-haem cytochrome c peroxidase from Pseudomonas aeruginosa==
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BACKGROUND: Cytochrome c peroxidase from Pseudomonas aeruginosa (PsCCP), represents a new class of peroxidases which work without the need to, create a semi-stable free radical for catalysis. The enzyme is located in, the bacterial periplasm where its likely function is to provide protection, against toxic peroxides. The soluble 323-residue single polypeptide chain, contains two covalent c-type haems with very different properties: one of, them is a low-potential (-330 mV) centre where hydrogen peroxide is, reduced (the peroxidatic site); the other is a high-potential (+320 mV), centre which feeds electrons to the peroxidatic site from soluble, electron-shuttle proteins such as cytochrome c and azurin. RESULTS: The, crystal structure of the oxidized form of PsCCP has been determined to 2.4, A resolution by multiple isomorphous replacement, and refined to an, R-factor of 19.2%. PsCCP is organized into two domains, both of them, containing a covalent c-haem in a structure reminiscent of class 1, cytochromes c. The domains are related by a quasi-twofold axis. The domain, interface holds a newly discovered calcium-binding site with an unusual, set of ligands. CONCLUSIONS: The likely function of the calcium site is to, maintain the structural integrity of the enzyme and/or to modulate, electron transfer between the two haem domains. The low-potential haem has, two histidine axial ligands (His55 and His71) and the high-potential haem, is ligated by His201 and Met275. There are no polar residues at the, peroxidatic site in the inactive oxidized enzyme. The structure suggests, that, in the half-reduced functional form of the enzyme, the low-potential, haem has to shed His71 in order to make the enzyme catalytically, competent. This process is likely to trigger a reorganization of the, active site, and may introduce a new residues into the haem pocket.
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<StructureSection load='1eb7' size='340' side='right'caption='[[1eb7]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1eb7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EB7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EB7 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1eb7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eb7 OCA], [https://pdbe.org/1eb7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eb7 RCSB], [https://www.ebi.ac.uk/pdbsum/1eb7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eb7 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CCPR_PSEAE CCPR_PSEAE] Catalyzes the peroxidative oxidation of azurin and cytochrome c551. Likely to provide protection against toxic peroxides.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/eb/1eb7_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1eb7 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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BACKGROUND: Cytochrome c peroxidase from Pseudomonas aeruginosa (PsCCP) represents a new class of peroxidases which work without the need to create a semi-stable free radical for catalysis. The enzyme is located in the bacterial periplasm where its likely function is to provide protection against toxic peroxides. The soluble 323-residue single polypeptide chain contains two covalent c-type haems with very different properties: one of them is a low-potential (-330 mV) centre where hydrogen peroxide is reduced (the peroxidatic site); the other is a high-potential (+320 mV) centre which feeds electrons to the peroxidatic site from soluble electron-shuttle proteins such as cytochrome c and azurin. RESULTS: The crystal structure of the oxidized form of PsCCP has been determined to 2.4 A resolution by multiple isomorphous replacement, and refined to an R-factor of 19.2%. PsCCP is organized into two domains, both of them containing a covalent c-haem in a structure reminiscent of class 1 cytochromes c. The domains are related by a quasi-twofold axis. The domain interface holds a newly discovered calcium-binding site with an unusual set of ligands. CONCLUSIONS: The likely function of the calcium site is to maintain the structural integrity of the enzyme and/or to modulate electron transfer between the two haem domains. The low-potential haem has two histidine axial ligands (His55 and His71) and the high-potential haem is ligated by His201 and Met275. There are no polar residues at the peroxidatic site in the inactive oxidized enzyme. The structure suggests that, in the half-reduced functional form of the enzyme, the low-potential haem has to shed His71 in order to make the enzyme catalytically competent. This process is likely to trigger a reorganization of the active site, and may introduce a new residues into the haem pocket.
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==About this Structure==
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Crystal structure of the di-haem cytochrome c peroxidase from Pseudomonas aeruginosa.,Fulop V, Ridout CJ, Greenwood C, Hajdu J Structure. 1995 Nov 15;3(11):1225-33. PMID:8591033<ref>PMID:8591033</ref>
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1EB7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=HEC:'>HEC</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Known structural/functional Sites: <scene name='pdbsite=401:Low-Potential+Peroxidatic+Haem+Centre+Covalently+Linked+...'>401</scene>, <scene name='pdbsite=402:High-Potential+Haem+Centre,+Accepts+Electrons+From+Donor+...'>402</scene> and <scene name='pdbsite=403:Ca-Binding+Site,'>403</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EB7 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Crystal structure of the di-haem cytochrome c peroxidase from Pseudomonas aeruginosa., Fulop V, Ridout CJ, Greenwood C, Hajdu J, Structure. 1995 Nov 15;3(11):1225-33. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8591033 8591033]
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</div>
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[[Category: Cytochrome-c peroxidase]]
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<div class="pdbe-citations 1eb7" style="background-color:#fffaf0;"></div>
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[[Category: Pseudomonas aeruginosa]]
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[[Category: Single protein]]
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[[Category: Fulop, V.]]
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[[Category: CA]]
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[[Category: HEC]]
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[[Category: electron transport]]
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[[Category: heme]]
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[[Category: oxidoreductase]]
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[[Category: peroxidase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:38:58 2008''
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==See Also==
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*[[Cytochrome c peroxidase 3D structures|Cytochrome c peroxidase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Pseudomonas aeruginosa]]
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[[Category: Fulop V]]

Current revision

Crystal structure of the di-haem cytochrome c peroxidase from Pseudomonas aeruginosa

PDB ID 1eb7

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