3OA7
Structure of the C-terminal domain of Cnm67, a core component of the spindle pole body of Saccharomyces cerevisiae
Summary for 3OA7
| Entry DOI | 10.2210/pdb3oa7/pdb |
| Descriptor | Head morphogenesis protein, Chaotic nuclear migration protein 67 fusion protein (2 entities in total) |
| Functional Keywords | coiled coils, structural protein, spindle pole body |
| Biological source | Bacillus phage phi29 (virus, yeast) More |
| Cellular location | Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body : P53865 |
| Total number of polymer chains | 1 |
| Total formula weight | 24281.71 |
| Authors | Klenchin, V.A.,Frye, J.J.,Rayment, I. (deposition date: 2010-08-04, release date: 2011-03-23, Last modification date: 2024-10-30) |
| Primary citation | Klenchin, V.A.,Frye, J.J.,Jones, M.H.,Winey, M.,Rayment, I. Structure-function analysis of the C-terminal domain of CNM67, a core component of the Saccharomyces cerevisiae spindle pole body. J.Biol.Chem., 286:18240-18250, 2011 Cited by PubMed Abstract: The spindle pole body of the budding yeast Saccharomyces cerevisiae has served as a model system for understanding microtubule organizing centers, yet very little is known about the molecular structure of its components. We report here the structure of the C-terminal domain of the core component Cnm67 at 2.3 Å resolution. The structure determination was aided by a novel approach to crystallization of proteins containing coiled-coils that utilizes globular domains to stabilize the coiled-coils. This enhances their solubility in Escherichia coli and improves their crystallization. The Cnm67 C-terminal domain (residues Asn-429-Lys-581) exhibits a previously unseen dimeric, interdigitated, all α-helical fold. In vivo studies demonstrate that this domain alone is able to localize to the spindle pole body. In addition, the structure reveals a large functionally indispensable positively charged surface patch that is implicated in spindle pole body localization. Finally, the C-terminal eight residues are disordered but are critical for protein folding and structural stability. PubMed: 21454609DOI: 10.1074/jbc.M111.227371 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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