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| | ==Leishmania major Peroxidase is a Cytochrome c Peroxidase== | | ==Leishmania major Peroxidase is a Cytochrome c Peroxidase== |
| - | <StructureSection load='4dy9' size='340' side='right' caption='[[4dy9]], [[Resolution|resolution]] 2.08Å' scene=''> | + | <StructureSection load='4dy9' size='340' side='right'caption='[[4dy9]], [[Resolution|resolution]] 2.08Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4dy9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Leima Leima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DY9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DY9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4dy9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Leishmania_major Leishmania major]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DY9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DY9 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.082Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LMJF_16_1310, LMJF_16_1320 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5664 LEIMA])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></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=4dy9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dy9 OCA], [http://pdbe.org/4dy9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4dy9 RCSB], [http://www.ebi.ac.uk/pdbsum/4dy9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4dy9 ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4dy9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dy9 OCA], [https://pdbe.org/4dy9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dy9 RCSB], [https://www.ebi.ac.uk/pdbsum/4dy9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dy9 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/Q4QEN5_LEIMA Q4QEN5_LEIMA]] Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.[RuleBase:RU004427] | + | [https://www.uniprot.org/uniprot/Q4QEN5_LEIMA Q4QEN5_LEIMA] Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.[RuleBase:RU004427] |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | Leishmania major peroxidase (LmP) exhibits both ascorbate and cytochrome c peroxidase activity. Our previous results illustrated that LmP has much higher activity against horse heart cytochrome c than ascorbate suggesting that cytochrome c may be the biologically important substrate. In order to elucidate the biological function of LmP, we have recombinantly expressed, purified and determined the 2.08A crystal structure of Leishmania major cytochrome c (LmCytc). Like other cytochromes c LmCytc has an electropositive surface surrounding the exposed heme edge that serves as the docking site with redox partners. LmCytc exhibits a unique UV-Visible reduced spectrum from most cytochromes because it has only one cysteine and therefore only one heme vinyl-thioether bond. Kinetic assays performed with LmCytc and LmP show that LmCytc is a much better substrate for LmP than horse heart cytochrome c. Furthermore, unlike the well-studied yeast system, the reaction follows classic Michaelis-Menten kinetics and is sensitive to increasing ionic strength. Using the yeast co-crystal as a control, protein-protein docking was performed using Rosetta to develop a model for the binding of LmP and LmCytc. These results suggest that the biological function of LmP is to act as a cytochrome c peroxidase.
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| - | LEISHMANIA MAJOR PEROXIDASE IS A CYTOCHROME C PEROXIDASE.,Jasion VS, Poulos TL Biochemistry. 2012 Feb 29. PMID:22372542<ref>PMID:22372542</ref>
| + | ==See Also== |
| - | | + | *[[Cytochrome C 3D structures|Cytochrome C 3D structures]] |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | *[[Cytochrome c peroxidase 3D structures|Cytochrome c peroxidase 3D structures]] |
| - | </div>
| + | |
| - | <div class="pdbe-citations 4dy9" style="background-color:#fffaf0;"></div>
| + | |
| - | == References ==
| + | |
| - | <references/>
| + | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Leima]] | + | [[Category: Large Structures]] |
| - | [[Category: Jasion, V S]] | + | [[Category: Leishmania major]] |
| - | [[Category: Poulos, T L]] | + | [[Category: Jasion VS]] |
| - | [[Category: Alpha helical bundle]] | + | [[Category: Poulos TL]] |
| - | [[Category: Electron transport]]
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| - | [[Category: Heme protein]]
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