5n22
From Proteopedia
Structure of xEco2 acetyltransferase domain bound to K106-CoA conjugate
Structural highlights
FunctionSMC3_XENLA Central component of cohesin, a complex required for chromosome cohesion during the cell cycle. The cohesin complex may form a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. Cohesion is coupled to DNA replication and is involved in DNA repair. The cohesin complex also plays an important role in spindle pole assembly during mitosis and in chromosomes movement.[1] Publication Abstract from PubMedSister-chromatid cohesion is established by Eco1-mediated acetylation on two conserved tandem lysines in the cohesin Smc3 subunit. However, the molecular basis of Eco1 substrate recognition and acetylation in cohesion is not fully understood. Here, we discover and rationalize the substrate specificity of Eco1 using mass spectrometry coupled with in-vitro acetylation assays and crystallography. Our structures of the X. laevis Eco2 (xEco2) bound to its primary and secondary Smc3 substrates demonstrate the plasticity of the substrate-binding site, which confers substrate specificity by concerted conformational changes of the central beta hairpin and the C-terminal extension. Structural Basis of Eco1-Mediated Cohesin Acetylation.,Chao WC, Wade BO, Bouchoux C, Jones AW, Purkiss AG, Federico S, O'Reilly N, Snijders AP, Uhlmann F, Singleton MR Sci Rep. 2017 Mar 14;7:44313. doi: 10.1038/srep44313. PMID:28290497[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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