5N1W
Structure of xEco2 acetyltransferase domain bound to K105-CoA conjugate
Summary for 5N1W
| Entry DOI | 10.2210/pdb5n1w/pdb |
| Descriptor | XEco2, ILE-GLY-ALA-LYX-LYS-ALA,ILE-GLY-ALA-LYX-LYS-ALA,ILE-GLY-ALA-LYX-LYS-ALA,ILE-GLY-ALA-LYX-LYS-ALA, MAGNESIUM ION, ... (5 entities in total) |
| Functional Keywords | cell cycle |
| Biological source | Xenopus laevis (African clawed frog) More |
| Total number of polymer chains | 4 |
| Total formula weight | 44815.78 |
| Authors | Chao, W.C.H.,Wade, B.O.,Singleton, M.R. (deposition date: 2017-02-06, release date: 2017-03-15, Last modification date: 2024-11-20) |
| Primary citation | Chao, W.C.,Wade, B.O.,Bouchoux, C.,Jones, A.W.,Purkiss, A.G.,Federico, S.,O'Reilly, N.,Snijders, A.P.,Uhlmann, F.,Singleton, M.R. Structural Basis of Eco1-Mediated Cohesin Acetylation. Sci Rep, 7:44313-44313, 2017 Cited by PubMed Abstract: 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 β hairpin and the C-terminal extension. PubMed: 28290497DOI: 10.1038/srep44313 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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