1XQ8
Human micelle-bound alpha-synuclein
Summary for 1XQ8
| Entry DOI | 10.2210/pdb1xq8/pdb |
| NMR Information | BMRB: 5744 |
| Descriptor | Alpha-synuclein (1 entity in total) |
| Functional Keywords | micelle-bound helix, lipid binding protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm: P37840 |
| Total number of polymer chains | 1 |
| Total formula weight | 14476.11 |
| Authors | Ulmer, T.S.,Bax, A.,Cole, N.B.,Nussbaum, R.L. (deposition date: 2004-10-11, release date: 2005-01-11, Last modification date: 2024-05-22) |
| Primary citation | Ulmer, T.S.,Bax, A.,Cole, N.B.,Nussbaum, R.L. Structure and dynamics of micelle-bound human alpha-synuclein J.Biol.Chem., 280:9595-9603, 2005 Cited by PubMed Abstract: Misfolding of the protein alpha-synuclein (aS), which associates with presynaptic vesicles, has been implicated in the molecular chain of events leading to Parkinson's disease. Here, the structure and dynamics of micelle-bound aS are reported. Val3-Val37 and Lys45-Thr92 form curved alpha-helices, connected by a well ordered, extended linker in an unexpected anti-parallel arrangement, followed by another short extended region (Gly93-Lys97), overlapping the recently identified chaperone-mediated autophagy recognition motif and a highly mobile tail (Asp98-Ala140). Helix curvature is significantly less than predicted based on the native micelle shape, indicating a deformation of the micelle by aS. Structural and dynamic parameters show a reduced helical content for Ala30-Val37. A dynamic variation in interhelical distance on the microsecond timescale is complemented by enhanced sub-nanosecond timescale dynamics, particularly in the remarkably glycine-rich segments of the helices. These unusually rich dynamics may serve to mitigate the effect of aS binding on membrane fluidity. The well ordered conformation of the helix-helix connector indicates a defined interaction with lipidic surfaces, suggesting that, when bound to larger diameter synaptic vesicles, it can act as a switch between this structure and a previously proposed uninterrupted helix. PubMed: 15615727DOI: 10.1074/jbc.M411805200 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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