3LLL
Crystal structure of mouse pacsin2 F-BAR domain
Summary for 3LLL
| Entry DOI | 10.2210/pdb3lll/pdb |
| Descriptor | Protein kinase C and casein kinase substrate in neurons protein 2, CALCIUM ION, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | coiled-coil, membrane fusion, vesicular traffic, cytoplasmic vesicle, endocytosis, phosphoprotein, sh3 domain |
| Biological source | Mus musculus (mouse) |
| Cellular location | Cytoplasmic vesicle (By similarity): Q9WVE8 |
| Total number of polymer chains | 2 |
| Total formula weight | 68765.14 |
| Authors | Rudolph, M.G. (deposition date: 2010-01-29, release date: 2010-05-26, Last modification date: 2023-09-06) |
| Primary citation | Plomann, M.,Wittmann, J.G.,Rudolph, M.G. A hinge in the distal end of the PACSIN 2 F-BAR domain may contribute to membrane-curvature sensing. J.Mol.Biol., 400:129-136, 2010 Cited by PubMed Abstract: The protein kinase C and casein kinase 2 substrates in neurons (PACSINs) represent a subfamily of membrane-binding proteins characterized by an amino-terminal Bin-Amphiphysin-Rvs (F-BAR) domain. PACSINs link membrane trafficking with actin dynamics and regulate the localization of distinct cargo molecules. The F-BAR domain forms a dimer essential for lipid binding. We have obtained crystals of authentic murine PACSIN 2 that contain an ordered F-BAR domain, indicating that additional domains are flexibly connected to F-BAR. The structure shares similarity to other BAR domains and exhibits special features unique to PACSINs. These include the uneven distribution of charged residues on the concave molecular surface and a so-called wedge loop that is driven into the membrane upon binding of PACSIN. The murine PACSIN 2 F-BAR domain requires dimerization for sensing of curved membranes, and the present structure also provides a mechanism for higher-order oligomer formation. Importantly, comparison of murine with human and Drosophila PACSIN 2 F-BAR domains reveals stark differences in the orientation of distal helical segments leading to a wider crescent shape of murine PACSIN 2. We define hinge residues for these movements that may help PACSINs sense and concomitantly reinforce membrane curvature. PubMed: 20471395DOI: 10.1016/j.jmb.2010.05.008 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.3 Å) |
Structure validation
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