NDLI: Structure and Orientation of a Voltage-Sensor Toxin in Lipid Membranes

Content Provider	PubMed Central
Author	Jung, Hyun Ho Jung, Hoi Jong Milescu, Mirela Lee, Chul Won Lee, Seungkyu Lee, Ju Yeon Eu, Young-jae Kim, Ha Hyung Swartz, Kenton J. Kim, Jae Il
Copyright Year	2010
Abstract	Amphipathic protein toxins from tarantula venom inhibit voltage-activated potassium (Kv) channels by binding to a critical helix-turn-helix motif termed the voltage sensor paddle. Although these toxins partition into membranes to bind the paddle motif, their structure and orientation within the membrane are unknown. We investigated the interaction of a tarantula toxin named SGTx with membranes using both fluorescence and NMR spectroscopy. Depth-dependent fluorescence-quenching experiments with brominated lipids suggest that Trp30 in SGTx is positioned ∼9 Å from the center of the bilayer. NMR spectra reveal that the inhibitor cystine knot structure of the toxin does not radically change upon membrane partitioning. Transferred cross-saturation NMR experiments indicate that the toxin's hydrophobic protrusion contacts the hydrophobic core of the membrane, whereas most surrounding polar residues remain at interfacial regions of the bilayer. The inferred orientation of the toxin reveals a twofold symmetry in the arrangement of basic and hydrophobic residues, a feature that is conserved among tarantula toxins. These results have important implications for regions of the toxin involved in recognizing membranes and voltage-sensor paddles, and for the mechanisms by which tarantula toxins alter the activity of different types of ion channels.
Related Links	http://dx.doi.org/10.1016/j.bpj.2010.04.061
Ending Page	646
Page Count	9
Starting Page	638
File Format	PDF
ISSN	00063495
e-ISSN	15420086
Journal	Biophysical Journal
Issue Number	2
Volume Number	99
Language	English
Publisher	The Biophysical Society
Publisher Date	2010-07-01
Access Restriction	Open
Rights Holder	The Biophysical Society
Subject Keyword	Biophysics Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Biophysics

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