3vf1: Difference between revisions
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==Structure of a calcium-dependent 11R-lipoxygenase suggests a mechanism for Ca-regulation== | ==Structure of a calcium-dependent 11R-lipoxygenase suggests a mechanism for Ca-regulation== | ||
<StructureSection load='3vf1' size='340' side='right' caption='[[3vf1]], [[Resolution|resolution]] 2.47Å' scene=''> | <StructureSection load='3vf1' size='340' side='right' caption='[[3vf1]], [[Resolution|resolution]] 2.47Å' scene=''> | ||
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<table><tr><td colspan='2'>[[3vf1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Gersemia_fruticosa Gersemia fruticosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VF1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VF1 FirstGlance]. <br> | <table><tr><td colspan='2'>[[3vf1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Gersemia_fruticosa Gersemia fruticosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VF1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VF1 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=SUC:SUCROSE'>SUC</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=SUC:SUCROSE'>SUC</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3vf1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vf1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vf1 RCSB], [http://www.ebi.ac.uk/pdbsum/3vf1 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3vf1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vf1 OCA], [http://pdbe.org/3vf1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3vf1 RCSB], [http://www.ebi.ac.uk/pdbsum/3vf1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3vf1 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3vf1" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 21:38, 11 August 2016
Structure of a calcium-dependent 11R-lipoxygenase suggests a mechanism for Ca-regulationStructure of a calcium-dependent 11R-lipoxygenase suggests a mechanism for Ca-regulation
Structural highlights
Publication Abstract from PubMedLipoxygenases (LOXs) are a key part of several signaling pathways that lead to inflammation and cancer. Yet, the mechanisms of substrate binding and allosteric regulation by the various LOX isoforms remain speculative. Here we report the 2.47 A resolution crystal structure of the arachidonate 11R-LOX from Gersemia fruticosa which sheds new light on the mechanism of LOX catalysis. Our crystallographic and mutational studies suggest that the aliphatic tail of the fatty acid is bound in a hydrophobic pocket with two potential entrances. We speculate that LOXs share a common T-shaped substrate channel architecture that gives rise to the varying positional specificities. A general allosteric mechanism is proposed for transmitting the activity-inducing effect of calcium binding from the membrane-targeting PLAT (polycystin-1/lipoxygenase/alpha-toxin) domain to the active site via a conserved pi-cation bridge. Structure of a calcium-dependent 11R-lipoxygenase suggests a mechanism for Ca2+-regulation.,Eek P, Jarving R, Jarving I, Gilbert NC, Newcomer ME, Samel N J Biol Chem. 2012 May 9. PMID:22573333[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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