Structural analysis of CYP53 P450s.

<p>3D-models for CYP53C2 from <i>Phanerochaete chrysosporium</i> (CYP53 Pchr) <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0107209#pone.0107209-Syed1" target="_blank">[4]</a> and CYP53A from <i>Thielavia terrestris</i> (CYP53 Tter) <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0107209#pone.0107209-Syed3" target="_blank">[24]</a> were constructed based on the template CYP51 from <i>Saccharomyces cerevisiae</i> (CYP51 Scer) (PDB ID: 4LXJ) <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0107209#pone.0107209-Monk1" target="_blank">[42]</a>. The CYP51 Scer crystal structure was downloaded from the Protein Data Bank (<a href="http://www.pdb.org" target="_blank">www.pdb.org</a>) with ID: 4LXJ. The overall structures of P450s were presented using PyMOL Molecular Graphics System, Version 1.7.1.1. Schrödinger, LLC (<a href="http://www.pymol.org/" target="_blank">http://www.pymol.org/</a>). The parameters used for validation of 3D-models of CYP53 Tte and CYP53 Pchr were presented in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0107209#pone-0107209-t003" target="_blank">Table 3</a>. The heme prosthetic group is shown in black color and the bound substrate for CYP53 Scer in green color. Alpha-helices and beta-strands are shown with blue and red. The membrane helix (MH) and the trans-membrane helix (TMH) are indicated in the models. P450 characteristics secondary structure notations are presented in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0107209#pone-0107209-g006" target="_blank">Fig. 6</a>.