1URU
Amphiphysin BAR domain from Drosophila
Summary for 1URU
| Entry DOI | 10.2210/pdb1uru/pdb |
| Descriptor | AMPHIPHYSIN (2 entities in total) |
| Functional Keywords | endocytosis, coiled-coil, membrane curvature |
| Biological source | DROSOPHILA MELANOGASTER (FRUIT FLY) |
| Total number of polymer chains | 1 |
| Total formula weight | 28269.15 |
| Authors | Evans, P.R.,Kent, H.M. (deposition date: 2003-11-06, release date: 2003-12-04, Last modification date: 2024-11-20) |
| Primary citation | Peter, B.J.,Kent, H.M.,Mills, I.G.,Vallis, Y.,Butler, J.G.,Evans, P.R.,Mcmahon, H.T. Bar Domains as Sensors of Membrane Curvature: The Amphiphysin Bar Structure Science, 303:495-, 2004 Cited by PubMed Abstract: The BAR (Bin/amphiphysin/Rvs) domain is the most conserved feature in amphiphysins from yeast to human and is also found in endophilins and nadrins. We solved the structure of the Drosophila amphiphysin BAR domain. It is a crescent-shaped dimer that binds preferentially to highly curved negatively charged membranes. With its N-terminal amphipathic helix and BAR domain (N-BAR), amphiphysin can drive membrane curvature in vitro and in vivo. The structure is similar to that of arfaptin2, which we find also binds and tubulates membranes. From this, we predict that BAR domains are in many protein families, including sorting nexins, centaurins, and oligophrenins. The universal and minimal BAR domain is a dimerization, membrane-binding, and curvature-sensing module. PubMed: 14645856DOI: 10.1126/SCIENCE.1092586 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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