3Q5D
crystal structure of human Atlastin-1 (residues 1-447) bound to GDP, crystal form 1
Summary for 3Q5D
| Entry DOI | 10.2210/pdb3q5d/pdb |
| Related | 3Q5E |
| Descriptor | Atlastin-1, GUANOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | g protein, gtpase, gdp/gtp binding, hydrolase |
| Biological source | Homo sapiens (human) |
| Cellular location | Endoplasmic reticulum membrane ; Multi- pass membrane protein : Q8WXF7 |
| Total number of polymer chains | 1 |
| Total formula weight | 52254.56 |
| Authors | Byrnes, L.J.,Sondermann, H. (deposition date: 2010-12-28, release date: 2011-01-19, Last modification date: 2017-11-08) |
| Primary citation | Byrnes, L.J.,Sondermann, H. Structural basis for the nucleotide-dependent dimerization of the large G protein atlastin-1/SPG3A. Proc.Natl.Acad.Sci.USA, 108:2216-2221, 2011 Cited by PubMed Abstract: The large GTPase atlastin belongs to the dynamin superfamily that has been widely implicated in facilitating membrane tubulation, fission, and in select cases, fusion. Mutations spread across atlastin isoform 1 (atlastin-1) have been identified in patients suffering from hereditary spastic paraplegia (HSP), a neurodegenerative disorder affecting motor neuron function in the lower extremities. On a molecular level, atlastin-1 associates with high membrane curvature and fusion events at the endoplasmic reticulum and cis-Golgi. Here we report crystal structures of atlastin-1 comprising the G and middle domains in two different conformations. Although the orientation of the middle domain relative to the G domain is different in the two structures, both reveal dimeric assemblies with a common, GDP-bound G domain dimer. In contrast, dimer formation in solution is observed only in the presence of GTP and transition state analogs, similar to other G proteins that are activated by nucleotide-dependent dimerization. Analyses of solution scattering data suggest that upon nucleotide binding, the protein adopts a somewhat extended, dimeric conformation that is reminiscent of one of the two crystal structures. These structural studies suggest a model for nucleotide-dependent regulation of atlastin with implications for membrane fusion. This mechanism is affected in several mutants associated with HSP, providing insights into disease pathogenesis. PubMed: 21220294DOI: 10.1073/pnas.1012792108 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.699 Å) |
Structure validation
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