6C1Z
Crystal structure of Apo Caenorhabditis elegans lipid binding protein 8 (LBP-8)
Summary for 6C1Z
| Entry DOI | 10.2210/pdb6c1z/pdb |
| Descriptor | Lipid Binding Protein, SULFATE ION (3 entities in total) |
| Functional Keywords | lbp8, lbp-8, fabp, fatty acid binding protein, lipid, lipid binding protein, lipid binding protein 8, c. elegans, caenorhabditis elegans, aging, lysosome, lipid transport, monounsaturated fatty acids, fatty acid |
| Biological source | Caenorhabditis elegans |
| Total number of polymer chains | 1 |
| Total formula weight | 16380.57 |
| Authors | Tillman, M.C.,Ortlund, E.A. (deposition date: 2018-01-05, release date: 2019-01-09, Last modification date: 2023-10-04) |
| Primary citation | Tillman, M.C.,Khadka, M.,Duffy, J.,Wang, M.C.,Ortlund, E.A. Structural characterization of life-extending Caenorhabditis elegans Lipid Binding Protein 8. Sci Rep, 9:9966-9966, 2019 Cited by PubMed Abstract: The lysosome plays a crucial role in the regulation of longevity. Lysosomal degradation is tightly coupled with autophagy that is induced by many longevity paradigms and required for lifespan extension. The lysosome also serves as a hub for signal transduction and regulates longevity via affecting nuclear transcription. One lysosome-to-nucleus retrograde signaling pathway is mediated by a lysosome-associated fatty acid binding protein LBP-8 in Caenorhabditis elegans. LBP-8 shuttles lysosomal lipids into the nucleus to activate lipid regulated nuclear receptors NHR-49 and NHR-80 and consequently promote longevity. However, the structural basis of LBP-8 action remains unclear. Here, we determined the first 1.3 Å high-resolution structure of this life-extending protein LBP-8, which allowed us to identify a structurally conserved nuclear localization signal and amino acids involved in lipid binding. Additionally, we described the range of fatty acids LBP-8 is capable of binding and show that it binds to life-extending ligands in worms such as oleic acid and oleoylethanolamide with high affinity. PubMed: 31292465DOI: 10.1038/s41598-019-46230-8 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.3 Å) |
Structure validation
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