3zil

Structure of the Wpl1 protein

spinqualitylabelsall models 3zil, resolution 2.01Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3zil is a 2 chain structure with sequence from Eremothecium gossypii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.012Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q75E93_ASHGO Publication Abstract from PubMed Correct segregation of duplicated chromosomes to daughter cells during mitosis requires the action of the cohesin complex. This tripartite ring-shaped molecule is involved in holding replicated sister chromatids together from S phase until anaphase onset. Establishment of stable cohesion involves acetylation of the Smc3 component of cohesin during replication by the Eco1 acetyltransferase. This has been proposed to antagonise the activity of another member of the cohesin complex, Wpl1. Here, we describe the X-ray structure of the conserved Wapl domain, and demonstrate that it binds the ATPase head of the Smc3 protein. We present data that suggest that Wpl1 may be involved in regulating the ATPase activity of cohesin, and that this may be subject to the acetylation state of Smc3. In addition, we present a structure of the Wapl domain bound to a functionally relevant segment of the Smc3 ATPase. Structural insights into the regulation of cohesion establishment by Wpl1.,Chatterjee A, Zakian S, Hu XW, Singleton MR EMBO J. 2013 Feb 8. doi: 10.1038/emboj.2013.16. PMID:23395900 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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