6ag5

Crystal structure of Ard1 N-terminal acetyltransferase E88H/H127E mutant from Sulfolobus solfataricusCrystal structure of Ard1 N-terminal acetyltransferase E88H/H127E mutant from Sulfolobus solfataricus

Structural highlights 6ag5 is a 1 chain structure with sequence from Sacs2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: , Gene: AsArd1 (SACS2) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The common mechanism of N-acetyltransferases (NATs) is a water-mediated catalysis, which is not conducive to thermophilic acetyltransferases. The crystal structure of SsArd1 shows an ordered catalytic water molecule in a trap formed by the residues H88 and E127. Structure-guided mutagenesis, kinetic studies and MD simulation indicated that the turnover rates of H88A, E127A and H88A/E127A mutants were low, but that of the H88E/E127H mutant could be restored to the level of the wild type. Adaptation of thermophilic acetyltransferase to a water-mediated catalytic mechanism.,Chang YY, Hagawa S, Hsu CH Chem Commun (Camb). 2020 Sep 10;56(72):10537-10540. doi: 10.1039/d0cc04305b. PMID:32780067 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 6ag5, resolution 2.32Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image