4UVK
Cohesin subunit Scc3 from Z. rouxii, 88-1035
Summary for 4UVK
| Entry DOI | 10.2210/pdb4uvk/pdb |
| Related | 4UVJ |
| Descriptor | ZYRO0D15994P (2 entities in total) |
| Functional Keywords | cell cycle, cohesin, mitosis, heat repeats, smc proteins |
| Biological source | ZYGOSACCHAROMYCES ROUXII |
| Total number of polymer chains | 1 |
| Total formula weight | 109749.08 |
| Authors | Roig, M.B.,Nasmyth, K.,Lowe, J. (deposition date: 2014-08-06, release date: 2014-08-20, Last modification date: 2024-05-08) |
| Primary citation | Roig, M.B.,Lowe, J.,Chan, K.L.,Beckouet, F.,Metson, J.,Nasmyth, K. Structure and Function of Cohesins Scc3/Sa Regulatory Subunit FEBS Lett., 588:3692-, 2014 Cited by PubMed Abstract: Sister chromatid cohesion involves entrapment of sister DNAs by a cohesin ring created through association of a kleisin subunit (Scc1) with ATPase heads of Smc1/Smc3 heterodimers. Cohesin's association with chromatin involves subunits recruited by Scc1: Wapl, Pds5, and Scc3/SA, in addition to Scc2/4 loading complex. Unlike Pds5, Wapl, and Scc2/4, Scc3s are encoded by all eukaryotic genomes. Here, a crystal structure of Scc3 reveals a hook-shaped protein composed of tandem α helices. Its N-terminal domain contains a conserved and essential surface (CES) present even in organisms lacking Pds5, Wapl, and Scc2/4, while its C-terminal domain binds a section of the kleisin Scc1. Scc3 turns over in G2/M while maintaining cohesin's association with chromosomes and it promotes de-acetylation of Smc3 upon Scc1 cleavage. PubMed: 25171859DOI: 10.1016/J.FEBSLET.2014.08.015 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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