|
|
| Line 1: |
Line 1: |
| | | | |
| | ==Crystal Structure of the Leishmania Major Peroxidase-Cytochrome C Complex== | | ==Crystal Structure of the Leishmania Major Peroxidase-Cytochrome C Complex== |
| - | <StructureSection load='4ged' size='340' side='right' caption='[[4ged]], [[Resolution|resolution]] 1.84Å' scene=''> | + | <StructureSection load='4ged' size='340' side='right'caption='[[4ged]], [[Resolution|resolution]] 1.84Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4ged]] is a 2 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=4GED OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GED FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4ged]] is a 2 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=4GED OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GED FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3riv|3riv]], [[4dy9|4dy9]]</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=4ged FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ged OCA], [https://pdbe.org/4ged PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ged RCSB], [https://www.ebi.ac.uk/pdbsum/4ged PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ged ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">APX, LMJF_34_0070 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5664 LEIMA]), 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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-ascorbate_peroxidase L-ascorbate peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.11 1.11.1.11] </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=4ged FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ged OCA], [http://pdbe.org/4ged PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ged RCSB], [http://www.ebi.ac.uk/pdbsum/4ged PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ged 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/Q4Q3K2_LEIMA Q4Q3K2_LEIMA] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 23: |
Line 20: |
| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Ascorbate peroxidase|Ascorbate peroxidase]] | + | *[[Ascorbate peroxidase 3D structures|Ascorbate peroxidase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: L-ascorbate peroxidase]] | + | [[Category: Large Structures]] |
| - | [[Category: Leima]] | + | [[Category: Leishmania major]] |
| - | [[Category: Doukov, T]] | + | [[Category: Doukov T]] |
| - | [[Category: Jasion, V S]] | + | [[Category: Jasion VS]] |
| - | [[Category: Li, H]] | + | [[Category: Li H]] |
| - | [[Category: Pineda, S H]] | + | [[Category: Pineda SH]] |
| - | [[Category: Poulos, T L]] | + | [[Category: Poulos TL]] |
| - | [[Category: Alpha helical bundle]]
| + | |
| - | [[Category: Cytochrome c peroxidase]]
| + | |
| - | [[Category: Heme peroxidase]]
| + | |
| - | [[Category: Oxidoreductase-electron transport complex]]
| + | |
| Structural highlights
Function
Q4Q3K2_LEIMA
Publication Abstract from PubMed
The causative agent of leishmaniasis is the protozoan parasite Leishmania major. Part of the host protective mechanism is the production of reactive oxygen species including hydrogen peroxide. In response, L. major produces a peroxidase, L. major peroxidase (LmP), that helps to protect the parasite from oxidative stress. LmP is a heme peroxidase that catalyzes the peroxidation of mitochondrial cytochrome c. We have determined the crystal structure of LmP in a complex with its substrate, L. major cytochrome c (LmCytc) to 1.84 A, and compared the structure to its close homolog, the yeast cytochrome c peroxidase-cytochrome c complex. The binding interface between LmP and LmCytc has one strong and one weak ionic interaction that the yeast system lacks. The differences between the steady-state kinetics correlate well with the Lm redox pair being more dependent on ionic interactions, whereas the yeast redox pair depends more on nonpolar interactions. Mutagenesis studies confirm that the ion pairs at the intermolecular interface are important to both k(cat) and K(M). Despite these differences, the electron transfer path, with respect to the distance between hemes, along the polypeptide chain is exactly the same in both redox systems. A potentially important difference, however, is the side chains involved. LmP has more polar groups (Asp and His) along the pathway compared with the nonpolar groups (Leu and Ala) in the yeast system, and as a result, the electrostatic environment along the presumed electron transfer path is substantially different.
Crystal structure of the Leishmania major peroxidase-cytochrome c complex.,Jasion VS, Doukov T, Pineda SH, Li H, Poulos TL Proc Natl Acad Sci U S A. 2012 Nov 6;109(45):18390-4. doi:, 10.1073/pnas.1213295109. Epub 2012 Oct 24. PMID:23100535[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Jasion VS, Doukov T, Pineda SH, Li H, Poulos TL. Crystal structure of the Leishmania major peroxidase-cytochrome c complex. Proc Natl Acad Sci U S A. 2012 Nov 6;109(45):18390-4. doi:, 10.1073/pnas.1213295109. Epub 2012 Oct 24. PMID:23100535 doi:http://dx.doi.org/10.1073/pnas.1213295109
|
