4XYH
Wild-type full length Mis16 in Schizosaccharomyces japonicus
Summary for 4XYH
| Entry DOI | 10.2210/pdb4xyh/pdb |
| Related | 4XYI |
| Descriptor | Kinetochore protein Mis16 (2 entities in total) |
| Functional Keywords | centromere, cenp-a, kinetochore, mis18 complex, histone, chaperone |
| Biological source | Schizosaccharomyces japonicus (strain yFS275 / FY16936) (Fission yeast) |
| Total number of polymer chains | 1 |
| Total formula weight | 48462.54 |
| Authors | An, S.,Kim, H.,Cho, U.-S. (deposition date: 2015-02-02, release date: 2016-01-13, Last modification date: 2023-09-27) |
| Primary citation | An, S.,Kim, H.,Cho, U.S. Mis16 Independently Recognizes Histone H4 and the CENP-ACnp1-Specific Chaperone Scm3sp. J.Mol.Biol., 427:3230-3240, 2015 Cited by PubMed Abstract: CENP-A is a centromere-specific histone H3 variant that is required for kinetochore assembly and accurate chromosome segregation. For it to function properly, CENP-A must be specifically localized to centromeres. In fission yeast, Scm3sp and the Mis18 complex, composed of Mis16, Eic1, and Mis18, function as a CENP-A(Cnp1)-specific chaperone and a recruiting factor, respectively, and together ensure accurate delivery of CENP-A(Cnp1) to centromeres. Although how Scm3sp specifically recognizes CENP-A(Cnp1) has been revealed recently, the recruiting mechanism of CENP-A(Cnp1) via the Mis18 complex remains unknown. In this study, we have determined crystal structures of Schizosaccharomyces japonicus Mis16 alone and in complex with the helix 1 of histone H4 (H4α1). Crystal structures followed by mutant analysis and affinity pull-downs have revealed that Mis16 recognizes both H4α1 and Scm3sp independently within the CENP-A(Cnp1)/H4:Scm3sp complex. This observation suggests that Mis16 gains CENP-A(Cnp1) specificity by recognizing both Scm3sp and histone H4. Our studies provide insights into the molecular mechanisms underlying specific recruitment of CENP-A(Cnp1)/H4:Scm3sp into centromeres. PubMed: 26343758DOI: 10.1016/j.jmb.2015.08.022 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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