1q5e

<table><tr><td colspan='2'>[[1q5e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"polyangium_compositum"_thaxter_1904 "polyangium compositum" thaxter 1904]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q5E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q5E FirstGlance]. <br>

</td></tr><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>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1pkf|1pkf]], [[1q5d|1q5d]]</div></td></tr>

[[https://www.uniprot.org/uniprot/C167_SORCE C167_SORCE]] Involved in the biosynthesis of epothilones, macrolactones which have a narrow anti-fungal spectrum and microtubule-stabilizing activity. Responsible for the epooxidation of epothilones C and D to epothilones A and B, respectively.<ref>PMID:10831849</ref>

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

Epothilones are potential anticancer drugs that stabilize microtubules by binding to tubulin in a manner similar to paclitaxel. Cytochrome P450epoK (P450epoK), a heme containing monooxygenase involved in epothilone biosynthesis in the myxobacterium Sorangium cellulosum, catalyzes the epoxidation of epothilones C and D into epothilones A and B, respectively. The 2.10-, 1.93-, and 2.65-A crystal structures reported here for the epothilone D-bound, epothilone B-bound, and substrate-free forms, respectively, are the first crystal structures of an epothilone-binding protein. Although the substrate for P450epoK is the largest of a P450 whose x-ray structure is known, the structural changes along with substrate binding or product release are very minor and the overall fold is similar to other P450s. The epothilones are positioned with the macrolide ring roughly perpendicular to the heme plane and I helix, and the thiazole moiety provides key interactions that very likely are critical in determining substrate specificity. Interestingly, there are strong parallels between the epothilone/P450epoK and paclitaxel/tubulin interactions. Based on structural similarities, a plausible epothilone tubulin-binding mode is proposed.

Crystal structures of epothilone D-bound, epothilone B-bound, and substrate-free forms of cytochrome P450epoK.,Nagano S, Li H, Shimizu H, Nishida C, Ogura H, Ortiz de Montellano PR, Poulos TL J Biol Chem. 2003 Nov 7;278(45):44886-93. Epub 2003 Aug 21. PMID:12933799<ref>PMID:12933799</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 1q5e" style="background-color:#fffaf0;"></div>

[[Category: Polyangium compositum thaxter 1904]]

[[Category: Li, H]]

[[Category: Montellano, P R.Ortiz de]]

[[Category: Nagano, S]]

[[Category: Nishida, C]]

[[Category: Ogura, H]]

[[Category: Poulos, T L]]

[[Category: Shimizu, H]]

[[Category: Cytochrome p450]]

[[Category: Oxidoreductase]]