6F46
Structure of the transmembrane helix of BclxL in phospholipid nanodiscs
Summary for 6F46
| Entry DOI | 10.2210/pdb6f46/pdb |
| NMR Information | BMRB: 27316 |
| Descriptor | Bcl-2-like protein 1 (1 entity in total) |
| Functional Keywords | nanodiscs, helix, apoptosis |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 3878.47 |
| Authors | Hagn, F.,Raltchev, K. (deposition date: 2017-11-29, release date: 2018-07-18, Last modification date: 2024-06-19) |
| Primary citation | Raltchev, K.,Pipercevic, J.,Hagn, F. Production and Structural Analysis of Membrane-Anchored Proteins in Phospholipid Nanodiscs. Chemistry, 24:5493-5499, 2018 Cited by PubMed Abstract: Structural studies on membrane-anchored proteins containing a transmembrane (TM) helix have been hampered by difficulties in producing these proteins in a natively folded form. Detergents that are required to solubilize the hydrophobic TM helix usually destabilize the soluble domain. Thus, TM helices are removed for structural studies, which neglects the pivotal role of a membrane on protein function. This work presents a versatile strategy for the production of this protein class attached to phospholipid nanodiscs. By inserting the TM-helix into nanodiscs and a subsequent SortaseA-mediated ligation of the soluble domain, membrane-anchored BclxL could be obtained in a folded conformation. This strategy is suitable for high-resolution structure determination as well as for probing membrane location by NMR. This method will be applicable to a wide range of membrane-anchored proteins and will be useful to decipher their functional role in a native membrane environment. PubMed: 29457664DOI: 10.1002/chem.201800812 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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