2N9B
Solution NMR Structure of Antiparallel Myosin-10:GCN4 Tandem Coiled-Coil
Summary for 2N9B
| Entry DOI | 10.2210/pdb2n9b/pdb |
| Related | 2ZTA 2lw9 |
| NMR Information | BMRB: 25899 |
| Descriptor | Unconventional myosin-X, General control protein GCN4 fusion (1 entity in total) |
| Functional Keywords | anti-parallel coiled-coil, coiled-coil, motor protein-transcription complex, motor protein/transcription |
| Biological source | Bos taurus (Bovine) More |
| Total number of polymer chains | 2 |
| Total formula weight | 16400.58 |
| Authors | Vavra, K.C.,Xia, Y.,Rock, R.S. (deposition date: 2015-11-12, release date: 2016-06-15, Last modification date: 2024-05-15) |
| Primary citation | Vavra, K.C.,Xia, Y.,Rock, R.S. Competition between Coiled-Coil Structures and the Impact on Myosin-10 Bundle Selection Biophys.J., 110:2517-2527, 2016 Cited by PubMed Abstract: Coiled-coil fusions are a useful approach to enforce dimerization in protein engineering. However, the final structures of coiled-coil fusion proteins have received relatively little attention. Here, we determine the structural outcome of adjacent parallel and antiparallel coiled coils. The targets are coiled coils that stabilize myosin-10 in single-molecule biophysical studies. We reveal the solution structure of a short, antiparallel, myosin-10 coiled-coil fused to the parallel GCN4-p1 coiled coil. Surprisingly, this structure is a continuous, antiparallel coiled coil where GCN4-p1 pairs with myosin-10 rather than itself. We also show that longer myosin-10 segments in these parallel/antiparallel fusions are dynamic and do not fold cooperatively. Our data resolve conflicting results on myosin-10 selection of actin filament bundles, demonstrating the importance of understanding coiled-coil orientation and stability. PubMed: 27276269DOI: 10.1016/j.bpj.2016.04.048 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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