Cryogenic electron tomography reveals helical organization of lipoprotein lipase in storage vesicles

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Kathryn H Gunn Anna Wheless Tom Calcraft Mark Kreutzberger Kareem El-Houshy Edward H Egelman Peter Rosenthal Saskia B Neher
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Abstract

Lipoprotein lipase (LPL) is a triglyceride lipase that is contained in intracellular vesicles in an inactive storage form before secretion, but the precise structural details have not yet been resolved. Using cryo-electron tomography (cryo-ET), we observe that LPL exists inside of storage vesicles as a filament with an 11-nanometer diameter and is packed in these vesicles in two distinct patterns. Next, we solved a 4.2-Å resolution cryo-electron microscopy (cryo-EM) structure of this 11-nanometer LPL filament using purified protein. The filament is made of repeating pairs of LPL molecules with occluded active sites, rendering the LPL inactive. The comparison of the in situ subtomogram average and the in vitro cryo-EM structure indicates that the previously uncharacterized physiological storage form of LPL is an inactive filament.

Journal details

Journal Science advances
Volume 11
Issue number 32
Pages eadx8711
Available online
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Publisher website (DOI) 10.1126/sciadv.adx8711
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Europe PubMed Central 40768583
Pubmed 40768583

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www.ebi.ac.uk/emdb/EMD-49737
www.ebi.ac.uk/emdb/EMD-49738

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