Predicting the structure of Anopheles gambiae cytochrome P450 protein using computational methods

Odia, Trust and Adebiyi, Marion (2015) Predicting the structure of Anopheles gambiae cytochrome P450 protein using computational methods. ISCB Africa ASBCB Conference on Bioinformatics.

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Abstract

the CYP12F4 pmtein is a membe1· of the Cytochmme P450 super-family of monooxygenanses, a la1·ge and dive1·se gmup of enzymes that catalyzes the oxidation of m·ganic substances and metabolic 1·eactions. It is found in the female Afdcan mosquito Anopheles gambiae (A. gambiae) that caiTies and tmnsmits the most deadly malada pamsite, Plasmodium falciparum (Pj). P1·esently expedmental sti·uctm·e is not available fo1· this p1·otein; it has thus 1·emained unchamctedzed with unknown function. This wo1·k employs in-silico methods to p1·edict the stmctm·e of this metabolic catalyzer and fm-the1· deduced a specific function fm· the same pmtein. Using 6 template pmteins, 29 1·esidues we1·e modeled with homology. Seveml web se1·ven we1·e deployed to p1·edict a computational model fm· CYP12F4. GOPET web tool was finally used to deduce the unique function of this pmtein. The folds we1·e identified and analyzed and the p1·otein was specifically found to be active in binding of molecules with 86% confidence value with vadous catalysis activities. 21 helices, 6 stmnds, 51 beta tum and 348 hydmgen bonds we1·e elucidated and analyzed on the stmctm·e. Seve1·al litemtm·es have confi1·med these findings. CYP12F4 is a heme and imn ion binding pmtein that caiTies heme and catalyses the incm·pomtion of one atom fmm molecula1· oxygen into a compound and 1·educes the othe1· atom of oxygen to watel". A deep undentanding of these pmpe1·ties of heme and its binding with 1·espect to CYP12F4 pmtein is vital in malada control.

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