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[[ | ==Leishmania major Peroxidase is a Cytochrome c Peroxidase== | ||
<StructureSection load='4dy9' size='340' side='right' caption='[[4dy9]], [[Resolution|resolution]] 2.08Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[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]. 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> | |||
</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> | |||
<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 Leishmania major])</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://www.rcsb.org/pdb/explore.do?structureId=4dy9 RCSB], [http://www.ebi.ac.uk/pdbsum/4dy9 PDBsum]</span></td></tr> | |||
</table> | |||
<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.,Jasion VS, Poulos TL Biochemistry. 2012 Feb 29. PMID:22372542<ref>PMID:22372542</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Cytochrome c|Cytochrome c]] | *[[Cytochrome c|Cytochrome c]] | ||
*[[Cytochrome c peroxidase|Cytochrome c peroxidase]] | |||
== | == References == | ||
< | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Leishmania major]] | [[Category: Leishmania major]] | ||
[[Category: Jasion, V S | [[Category: Jasion, V S]] | ||
[[Category: Poulos, T L | [[Category: Poulos, T L]] | ||
[[Category: Alpha helical bundle]] | [[Category: Alpha helical bundle]] | ||
[[Category: Electron transport]] | [[Category: Electron transport]] | ||
[[Category: Heme protein]] | [[Category: Heme protein]] | ||