ArticleBiophysical journal2012
Locating a lipid at the portal to the lipoxygenase active site.
Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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26 citing papers in PubMed, 62 citations in OpenAlex.
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- Comparative kinetic isotope effects on first- and second-order rate constants of soybean lipoxygenase variants uncover a substrate-binding network.The Journal of biological chemistry · 2019Article
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- The contribution of modern EPR to structural biology.Emerging topics in life sciences · 2018Article
- Hydrogen-deuterium exchange reveals long-range dynamical allostery in soybean lipoxygenase.The Journal of biological chemistry · 2018Article
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- Studying the Conformation of a Receptor Tyrosine Kinase in Solution by Inhibitor-Based Spin Labeling.Angewandte Chemie (International ed. in English) · 2017Article
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- Mechanism of influenza A M2 transmembrane domain assembly in lipid membranes.Scientific reports · 2015Article
- Combination of X-ray crystallography, SAXS and DEER to obtain the structure of the FnIII-3,4 domains of integrin α6β4.Acta crystallographica. Section D, Biological crystallography · 2015Article
- The structural basis for specificity in lipoxygenase catalysis.Protein science : a publication of the Protein Society · 2015Review
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6 authors at 3 institutions in 1 country.
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Abstract
Lipoxygenase enzymes initiate diverse signaling pathways by specifically directing oxygen to different carbons of arachidonate and other polyunsaturated acyl chains, but structural origins of this specificity have remained unclear. We therefore determined the nature of the lipoxygenase interaction with the polar-end of a paramagnetic lipid by electron paramagnetic resonance spectroscopy. Distances between selected grid points on soybean seed lipoxygenase-1 (SBL1) and a lysolecithin spin-labeled on choline were measured by pulsed (electron) dipolar spectroscopy. The protein grid was designed by structure-based modeling so that five natural side chains were replaced with spin labels. Pairwise distances in 10 doubly spin-labeled mutants were examined by pulsed dipolar spectroscopy, and a fit to the model was optimized. Finally, experimental distances between the lysolecithin spin and each single spin site on SBL1 were also obtained. With these 15 distances, distance geometry localized the polar-end and the spin of the lysolecithin to the region between the two domains in the SBL1 structure, nearest to E236, K260, Q264, and Q544. Mutation of a nearby residue, E256A, relieved the high pH requirement for enzyme activity of SBL1 and allowed lipid binding at pH 7.2. This general approach could be used to locate other flexible molecules in macromolecular complexes.
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