5AR1
Crystal structure of Cdc11 from Saccharomyces cerevisiae
Summary for 5AR1
| Entry DOI | 10.2210/pdb5ar1/pdb |
| Descriptor | CELL DIVISION CONTROL PROTEIN 11 (1 entity in total) |
| Functional Keywords | cell cycle, spetins, yeast, cdc11, nucleotide binding |
| Biological source | SACCHAROMYCES CEREVISIAE (BAKER'S YEAST) |
| Cellular location | Membrane : P32458 |
| Total number of polymer chains | 1 |
| Total formula weight | 34611.72 |
| Authors | Brausemann, A.,Gerhardt, S.,Schott, A.K.,Einsle, O.,Grosse-Berkenbusch, A.,Johnsson, N.,Gronemeyer, T. (deposition date: 2015-09-23, release date: 2016-01-27, Last modification date: 2024-01-10) |
| Primary citation | Brausemann, A.,Gerhardt, S.,Schott, A.K.,Einsle, O.,Grosse-Berkenbusch, A.,Johnsson, N.,Gronemeyer, T. Crystal Structure of Cdc11, a Septin Subunit from Saccharomyces Cerevisiae. J.Struct.Biol., 193:157-, 2016 Cited by PubMed Abstract: Septins are a conserved family of GTP-binding proteins that assemble into a highly ordered array of filaments at the mother bud neck in Saccharomyces cerevisiae cells. Many molecular functions and mechanisms of the septins in S. cerevisiae were already uncovered. However, structural information is only available from modeling the crystallized subunits of the human septins into the EM cryomicroscopy data of the yeast hetero-octameric septin rod. Octameric rods are the building block of septin filaments in yeast. We present here the first crystal structure of Cdc11, the terminal subunit of the octameric rod and discuss its structure in relation to its human homologues. Size exclusion chromatography analysis revealed that Cdc11 forms homodimers through its C-terminal coiled coil tail. PubMed: 26780475DOI: 10.1016/J.JSB.2016.01.004 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.85 Å) |
Structure validation
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