| First Author | Yu RC | Year | 1999 |
| Journal | Mol Cell | Volume | 4 |
| Issue | 1 | Pages | 97-107 |
| PubMed ID | 10445031 | Mgi Jnum | J:56708 |
| Mgi Id | MGI:1342202 | Doi | 10.1016/s1097-2765(00)80191-4 |
| Citation | Yu RC, et al. (1999) NSF N-terminal domain crystal structure: models of NSF function. Mol Cell 4(1):97-107 |
| abstractText | N-ethylmaleimide-sensitive factor (NSF) is a hexameric ATPase essential for eukaryotic vesicle fusion. Along with SNAP proteins, it disassembles cis-SNARE complexes upon ATP hydrolysis, preparing SNAREs for trans complex formation. We have determined the crystal structure of the N-terminal domain of NSF (N) to 1.9 A resolution. N contains two subdomains which form a groove that is a likely SNAP interaction site. Unexpectedly, both N subdomains are structurally similar to domains in EF-Tu. Based on this similarity, we propose a model for a large conformational change in NSF that drives SNARE complex disassembly. |
