2DOQ
crystal structure of Sfi1p/Cdc31p complex
Summary for 2DOQ
| Entry DOI | 10.2210/pdb2doq/pdb |
| Descriptor | Cell division control protein 31, SFI1p, CALCIUM ION, ... (4 entities in total) |
| Functional Keywords | sfi1p, centrin, cdc31p, spindle pole body, centrosome, cell cycle |
| Biological source | Saccharomyces cerevisiae (baker's yeast) More |
| Cellular location | Nucleus, nuclear pore complex: P06704 Cytoplasm, cytoskeleton, spindle pole : Q12369 |
| Total number of polymer chains | 4 |
| Total formula weight | 68844.34 |
| Authors | Li, S.,Sandercock, A.M.,Conduit, P.T.,Robinson, C.V.,Williams, R.L.,Kilmartin, J.V. (deposition date: 2006-05-03, release date: 2006-06-27, Last modification date: 2024-10-30) |
| Primary citation | Li, S.,Sandercock, A.M.,Conduit, P.,Robinson, C.V.,Williams, R.L.,Kilmartin, J.V. Structural role of Sfi1p-centrin filaments in budding yeast spindle pole body duplication. J.Cell Biol., 173:867-877, 2006 Cited by PubMed Abstract: Centrins are calmodulin-like proteins present in centrosomes and yeast spindle pole bodies (SPBs) and have essential functions in their duplication. The Saccharomyces cerevisiae centrin, Cdc31p, binds Sfi1p on multiple conserved repeats; both proteins localize to the SPB half-bridge, where the new SPB is assembled. The crystal structures of Sfi1p-centrin complexes containing several repeats show Sfi1p as an alpha helix with centrins wrapped around each repeat and similar centrin-centrin contacts between each repeat. Electron microscopy (EM) shadowing of an Sfi1p-centrin complex with 15 Sfi1 repeats and 15 centrins bound showed filaments 60 nm long, compatible with all the Sfi1 repeats as a continuous alpha helix. Immuno-EM localization of the Sfi1p N and C termini showed Sfi1p-centrin filaments spanning the length of the half-bridge with the Sfi1p N terminus at the SPB. This suggests a model for SPB duplication where the half-bridge doubles in length by association of the Sfi1p C termini, thereby providing a new Sfi1p N terminus to initiate SPB assembly. PubMed: 16785321DOI: 10.1083/jcb.200603153 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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