2N93
Solution structure of lcFABP
Summary for 2N93
| Entry DOI | 10.2210/pdb2n93/pdb |
| NMR Information | BMRB: 25400 |
| Descriptor | Fatty acid-binding protein (1 entity in total) |
| Functional Keywords | lipid binding protein |
| Biological source | Luciola cerata |
| Total number of polymer chains | 1 |
| Total formula weight | 14450.55 |
| Authors | |
| Primary citation | Tseng, K.L.,Lee, Y.Z.,Chen, Y.R.,Lyu, P.C. 1H, 15N and 13C resonance assignments of light organ-associated fatty acid-binding protein of Taiwanese fireflies. Biomol NMR Assign, 10:71-74, 2016 Cited by PubMed Abstract: Fatty acid-binding proteins (FABPs) are a family of proteins that modulate the transfer of various fatty acids in the cytosol and constitute a significant portion in many energy-consuming cells. The ligand binding properties and specific functions of a particular type of FABP seem to be diverse and depend on the respective binding cavity as well as the cell type from which this protein is derived. Previously, a novel FABP (lcFABP; lc: Luciola cerata) was identified in the light organ of Taiwanese fireflies. The lcFABP was proved to possess fatty acids binding capabilities, especially for fatty acids of length C14-C18. However, the structural details are unknown, and the structure-function relationship has remained to be further investigated. In this study, we finished the (1)H, (15)N and (13)C chemical shift assignments of (15)N/(13)C-enriched lcFABP by solution NMR spectroscopy. In addition, the secondary structure distribution was revealed based on the backbone N, H, Cα, Hα, C and side chain Cβ assignments. These results can provide the basis for further structural exploration of lcFABP. PubMed: 26373428DOI: 10.1007/s12104-015-9640-0 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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