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4UVK

Cohesin subunit Scc3 from Z. rouxii, 88-1035

Summary for 4UVK
Entry DOI10.2210/pdb4uvk/pdb
Related4UVJ
DescriptorZYRO0D15994P (2 entities in total)
Functional Keywordscell cycle, cohesin, mitosis, heat repeats, smc proteins
Biological sourceZYGOSACCHAROMYCES ROUXII
Total number of polymer chains1
Total formula weight109749.08
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 citationRoig, 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: 25171859
DOI: 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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