Low resolution structural studies of Munc18c complexed with a Syntaxin-4/T4- Lysozyme Fusion
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Date
2016-11-29
Journal Title
Journal ISSN
Volume Title
Publisher
Australian Institute of Nuclear Science and Engineering
Abstract
Soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNARE) act at every intracellular trafficking pathway. Cognate v-SNAREs (e.g. VAMP) and t-SNAREs (Syntaxin (Sx) and SNAP) form a high affinity SNARE ternary complex (Sx-SNAP-VAMP) that brings the membranes together, triggering fusion. Syntaxins consist of a SNARE motif, and a three-helix bundle. In an open confirmation, the SNARE motif is free to form the SNARE ternary complex (stimulating fusion), but in the closed confirmation fusion is inhibited. Sec1p/Munc18 (SM) proteins bind to Sx, regulating SNARE mediated fusion [1], but their exact role is not well understood [2-4]. In the cell, Sx is bound to the membrane, and it is possible that this tethering may influence
the manner in which it interacts with other proteins. As a means of investigating structural changes arising due to tethering, here, we investigate how the addition of a C-terminal T4-Lysozyme (soluble) fusion to Sx4 modulates its interaction with Munc18c. Preliminary low-resolution models of the Munc18c-Sx4T4 complex optimized against small-angle scattering data will be presented.
Description
Keywords
Proteins, Receptors, Membrane proteins, Small angle scattering, Resolution, Complexes
Citation
Whitten, A. E., Rehman, A., Hu, S.-H., Tnimov, Z., Christie, M. P., King, G. J., Jarrott, R. J., Norwood, S., Alexandrov, K., Collins, B. M., & Martin, J. L. (2016). Low resolution structural studies of Munc18c complexed with a Syntaxin-4/T4- Lysozyme Fusion. Paper presented at 13th AINSE-ANBUG Neutron Scattering Symposium, Sydney, NSW, Australia, 29-30 November 2016.