8ERL
CryoEM Structure of Lipoprotein Lipase Dimer
Summary for 8ERL
| Entry DOI | 10.2210/pdb8erl/pdb |
| EMDB information | 28554 |
| Descriptor | Lipoprotein lipase (1 entity in total) |
| Functional Keywords | dimer, lipase, hydrolase |
| Biological source | Bos taurus (cattle) |
| Total number of polymer chains | 2 |
| Total formula weight | 106897.58 |
| Authors | Gunn, K.H.,Neher, S.B. (deposition date: 2022-10-12, release date: 2023-05-03, Last modification date: 2025-05-21) |
| Primary citation | Gunn, K.H.,Neher, S.B. Structure of dimeric lipoprotein lipase reveals a pore adjacent to the active site. Nat Commun, 14:2569-2569, 2023 Cited by PubMed Abstract: Lipoprotein lipase (LPL) hydrolyzes triglycerides from circulating lipoproteins, releasing free fatty acids. Active LPL is needed to prevent hypertriglyceridemia, which is a risk factor for cardiovascular disease (CVD). Using cryogenic electron microscopy (cryoEM), we determined the structure of an active LPL dimer at 3.9 Å resolution. This structure reveals an open hydrophobic pore adjacent to the active site residues. Using modeling, we demonstrate that this pore can accommodate an acyl chain from a triglyceride. Known LPL mutations that lead to hypertriglyceridemia localize to the end of the pore and cause defective substrate hydrolysis. The pore may provide additional substrate specificity and/or allow unidirectional acyl chain release from LPL. This structure also revises previous models on how LPL dimerizes, revealing a C-terminal to C-terminal interface. We hypothesize that this active C-terminal to C-terminal conformation is adopted by LPL when associated with lipoproteins in capillaries. PubMed: 37142573DOI: 10.1038/s41467-023-38243-9 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.9 Å) |
Structure validation
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