Abstract
Apolipophorin III, a 163 residue monomeric protein from the greater wax moth Galleria mellonella (abbreviated as apoLp-IIIGM), has roles in upregulating expression of antimicrobial proteins as well as binding and deforming bacterial membranes. Due to its similarity to vertebrate apolipoproteins there is interest in performing atomic resolution analysis of apoLp-IIIGM as part of an effort to better understand its mechanism of action in innate immunity. In the first step towards structural characterization of apoLp-IIIGM, 99 % of backbone and 88 % of side chain 1H, 13C and 15N chemical shifts were assigned. TALOS+ analysis of the backbone resonances has predicted that the protein is composed of five long helices, which is consistent with the reported structures of apolipophorins from other insect species. The next stage in the characterization of apoLp-III from G. mellonella will be to utilize these resonance assignments in solving the solution structure of this protein.
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Acknowledgments
Research reported in this publication was supported by the National Institute of General Medical Sciences of the National Institutes of Health (Award Number SC3GM089564 to PMMW), and by a Major Research Instrumentation grant for a 600 MHz NMR spectrometer provided by the National Science Foundation (Award Number CHE-1040134 to KAC).
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Crowhurst, K.A., Horn, J.V. & Weers, P.M. Backbone and side chain chemical shift assignments of apolipophorin III from Galleria mellonella . Biomol NMR Assign 10, 143–147 (2016). https://doi.org/10.1007/s12104-015-9654-7
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DOI: https://doi.org/10.1007/s12104-015-9654-7