5n1w

Structure of xEco2 acetyltransferase domain bound to K105-CoA conjugate

spinqualitylabelsall models 5n1w, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5n1w is a 4 chain structure with sequence from Xenopus laevis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Ligands: 8HB, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A8QZK6_XENLA Publication Abstract from PubMed Sister-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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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