1pkf: Difference between revisions

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-[[Image:1pkf.jpg|left|200px]]
-<!--
+==Crystal Structure of Epothilone D-bound Cytochrome P450epoK==
-The line below this paragraph, containing "STRUCTURE_1pkf", creates the "Structure Box" on the page.
+<StructureSection load='1pkf' size='340' side='right'caption='[[1pkf]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1pkf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sorangium_cellulosum Sorangium cellulosum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PKF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PKF FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPD:EPOTHILONE+D'>EPD</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
-{{STRUCTURE_1pkf|  PDB=1pkf  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1pkf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pkf OCA], [https://pdbe.org/1pkf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pkf RCSB], [https://www.ebi.ac.uk/pdbsum/1pkf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pkf ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pk/1pkf_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1pkf ConSurf].
+<div style="clear:both"></div>
-'''Crystal Structure of Epothilone D-bound Cytochrome P450epoK'''
+==See Also==
+*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]]
+== References ==
-==Overview==
+<references/>
-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.
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-PKF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sorangium_cellulosum Sorangium cellulosum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PKF OCA].
-==Reference==
-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:[http://www.ncbi.nlm.nih.gov/pubmed/12933799 12933799]
-[[Category: Single protein]]
 [[Category: Sorangium cellulosum]]
-[[Category: Li, H.]]
+[[Category: Li H]]
-[[Category: Montellano, P R.Ortiz de.]]
+[[Category: Nagano S]]
-[[Category: Nagano, S.]]
+[[Category: Nishida C]]
-[[Category: Nishida, C.]]
+[[Category: Ogura H]]
-[[Category: Ogura, H.]]
+[[Category: Ortiz de Montellano PR]]
-[[Category: Poulos, T L.]]
+[[Category: Poulos TL]]
-[[Category: Shimizu, H.]]
+[[Category: Shimizu H]]
-[[Category: Cytochrome p450epok]]
-[[Category: Heme-enzyme]]
-[[Category: Oxidoreductase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 05:11:17 2008''