6XJ1
Crystal Structure of CDC15 F-BAR Domain from Schizosaccharomyces pombe
Summary for 6XJ1
| Entry DOI | 10.2210/pdb6xj1/pdb |
| Descriptor | Cell division control protein 15 (2 entities in total) |
| Functional Keywords | cell division control protein 15, cytoskeletal protein binding, cytoskeletal protein membrane adaptor, phospholipid binding, cell cycle |
| Biological source | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
| Total number of polymer chains | 2 |
| Total formula weight | 68074.45 |
| Authors | Chandra, M.,Jackson, L.P.,Snider, C.E.,Gould, K.L. (deposition date: 2020-06-22, release date: 2020-12-16, Last modification date: 2023-10-18) |
| Primary citation | Snider, C.E.,Chandra, M.,McDonald, N.A.,Willet, A.H.,Collier, S.E.,Ohi, M.D.,Jackson, L.P.,Gould, K.L. Opposite Surfaces of the Cdc15 F-BAR Domain Create a Membrane Platform That Coordinates Cytoskeletal and Signaling Components for Cytokinesis. Cell Rep, 33:108526-108526, 2020 Cited by PubMed Abstract: Many eukaryotes assemble an actin- and myosin-based cytokinetic ring (CR) on the plasma membrane (PM) for cell division, but how it is anchored there remains unclear. In Schizosaccharomyces pombe, the F-BAR protein Cdc15 links the PM via its F-BAR domain to proteins in the CR's interior via its SH3 domain. However, Cdc15's F-BAR domain also directly binds formin Cdc12, suggesting that Cdc15 may polymerize a protein network directly adjacent to the membrane. Here, we determine that the F-BAR domain binds Cdc12 using residues on the face opposite its membrane-binding surface. These residues also bind paxillin-like Pxl1, promoting its recruitment with calcineurin to the CR. Mutation of these F-BAR domain residues results in a shallower CR, with components localizing ∼35% closer to the PM than in wild type, and aberrant CR constriction. Thus, F-BAR domains serve as oligomeric membrane-bound platforms that can modulate the architecture of an entire actin structure. PubMed: 33357436DOI: 10.1016/j.celrep.2020.108526 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.52 Å) |
Structure validation
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