4dy9: Difference between revisions

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[[Image:4dy9.jpg|left|200px]]


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==Leishmania major Peroxidase is a Cytochrome c Peroxidase==
The line below this paragraph, containing "STRUCTURE_4dy9", creates the "Structure Box" on the page.
<StructureSection load='4dy9' size='340' side='right'caption='[[4dy9]], [[Resolution|resolution]] 2.08&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.082&#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=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
{{STRUCTURE_4dy9|  PDB=4dy9  |  SCENE=  }}
<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>
== Function ==
[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.


===Leishmania major Peroxidase is a Cytochrome c Peroxidase===
LEISHMANIA MAJOR PEROXIDASE IS A CYTOCHROME C PEROXIDASE.,Jasion VS, Poulos TL Biochemistry. 2012 Feb 29. PMID:22372542<ref>PMID:22372542</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4dy9" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_22372542}}, adds the Publication Abstract to the page
*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 22372542 is the PubMed ID number.
*[[Cytochrome c peroxidase 3D structures|Cytochrome c peroxidase 3D structures]]
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== References ==
{{ABSTRACT_PUBMED_22372542}}
<references/>
 
__TOC__
==About this Structure==
</StructureSection>
[[4dy9]] is a 1 chain structure with sequence from [http://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].
[[Category: Large Structures]]
 
==Reference==
<ref group="xtra">PMID:022372542</ref><references group="xtra"/>
[[Category: Leishmania major]]
[[Category: Leishmania major]]
[[Category: Jasion, V S.]]
[[Category: Jasion VS]]
[[Category: Poulos, T L.]]
[[Category: Poulos TL]]
[[Category: Alpha helical bundle]]
[[Category: Electron transport]]
[[Category: Heme protein]]

Latest revision as of 10:49, 13 August 2026

Leishmania major Peroxidase is a Cytochrome c Peroxidase

4dy9, resolution 2.08Å

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