View source for 5mef


==Cyanothece lipoxygenase 2 (CspLOX2) variant - L304F==
<StructureSection load='5mef' size='340' side='right'caption='[[5mef]], [[Resolution|resolution]] 2.36&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5mef]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rippkaea_orientalis_PCC_8801 Rippkaea orientalis PCC 8801]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MEF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MEF FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.357&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5mef FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mef OCA], [https://pdbe.org/5mef PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mef RCSB], [https://www.ebi.ac.uk/pdbsum/5mef PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mef ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/B7JX99_RIPO1 B7JX99_RIPO1] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The biological function of lipoxygenases depends on the regio and stereo specific formation of fatty acid-derived hydroperoxides and different concepts exist to explain the mechanism that directs dioxygen to a specific carbon atom within the substrate. Here, we report the 1.8 A resolution crystal structure of a cyanobacterial lipoxygenase that produces bis-allylic hydroperoxides (CspLOX2). Site directed mutagenesis experiments combined with computational approaches reveal that residues around the active site direct dioxygen to a preferred carbon atom and stereo configuration in the substrate fatty acid. Modulating the cavity volume around the pentadiene system of linoleic acid shifted the product formation towards 9S-, 9R-, 13S- or 13R-hydroperoxides in correlation with the site of mutation, thus decreasing the amount of the bis-allylic 11R-hydroperoxide. Decreasing the channel size of a 9R-lipoxygenase (CspLOX1) on the other hand could in turn induce formation of the bis-allylic 11R-hydroperoxide. Together this study suggests that an active site clamp fixing the pentadiene system of the substrate together with steric shielding controls the stereo and regio specific positioning of dioxygen at all positions of the reacting pentadiene system of substrate fatty acids.

Lipoxygenase 2 from Cyanothece sp. controls dioxygen insertion by steric shielding and substrate fixation.,Newie J, Neumann P, Werner M, Mata RA, Ficner R, Feussner I Sci Rep. 2017 May 18;7(1):2069. doi: 10.1038/s41598-017-02153-w. PMID:28522865<ref>PMID:28522865</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5mef" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rippkaea orientalis PCC 8801]]
[[Category: Feussner I]]
[[Category: Ficner R]]
[[Category: Mata RA]]
[[Category: Neumann P]]
[[Category: Newie J]]
[[Category: Werner M]]