Journal:Acta Cryst F:S2053230X20011310
From Proteopedia
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Here we present the crystallization and first structure of human IMPase covalently complexed with ebselen, a 1.47 Å crystal structure (PDB entry [[6zk0]]). In the human-IMPase-complex ebselen, in a ring opened conformation, is covalently attached to Cys141, a residue located away from the active site. | Here we present the crystallization and first structure of human IMPase covalently complexed with ebselen, a 1.47 Å crystal structure (PDB entry [[6zk0]]). In the human-IMPase-complex ebselen, in a ring opened conformation, is covalently attached to Cys141, a residue located away from the active site. | ||
| - | IMPase is a dimeric enzyme and, in the crystal structure, two adjacent dimers share four ebselen molecules, creating a tetramer with ~222 symmetry. In the crystal structure presented in this publication, the active site in the tetramer is still accessible, suggesting that ebselen may function as an allosteric inhibitor, or may block the binding of partner proteins. | + | IMPase is a dimeric enzyme and, in the crystal structure, two adjacent dimers share four ebselen molecules, creating a tetramer with ~222 symmetry. In the crystal structure presented in this publication, the active site in the tetramer is still accessible, suggesting that ebselen may function as an allosteric inhibitor, or may block the binding of partner proteins. <scene name='85/859036/Cv/12'>TextToBeDisplayed</scene> |
Orthogonal views of IMPase dimer showing ebselen on Cys141 and metal ions in the active sites based on the structure of PDB entry [[6zk0]]: | Orthogonal views of IMPase dimer showing ebselen on Cys141 and metal ions in the active sites based on the structure of PDB entry [[6zk0]]: | ||
Revision as of 13:31, 23 August 2020
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