4DY9

Leishmania major Peroxidase is a Cytochrome c Peroxidase

Summary for 4DY9

• Entry DOI: 10.2210/pdb4dy9/pdb
• Descriptor: Cytochrome c, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• Functional Keywords: alpha helical bundle, electron transport, heme protein
• Biological source: Leishmania major
• Total number of polymer chains: 1
• Total formula weight: 12822.56

Authors

Jasion, V.S.,Poulos, T.L. (deposition date: 2012-02-28, release date: 2012-03-14, Last modification date: 2024-04-03)

Primary citation

Jasion, V.S.,Poulos, T.L.
Leishmania major Peroxidase Is a Cytochrome c Peroxidase.
Biochemistry, 51:2453-2460, 2012

PubMed Abstract: Leishmania major peroxidase (LmP) exhibits both ascorbate and cytochrome c peroxidase activities. Our previous results illustrated that LmP has a much higher activity against horse heart cytochrome c than ascorbate, suggesting that cytochrome c may be the biologically important substrate. To elucidate the biological function of LmP, we have recombinantly expressed, purified, and determined the 2.08 Å crystal structure of L. major cytochrome c (LmCytc). Like other types of cytochrome c, LmCytc has an electropositive surface surrounding the exposed heme edge that serves as the site of docking with redox partners. 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 an increasing ionic strength. Using the yeast cocrystal 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.

PubMed: 22372542
DOI: 10.1021/bi300169x

Experimental method

X-RAY DIFFRACTION (2.082 Å)