6AG5

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

Summary for 6AG5

Entry DOI	10.2210/pdb6ag5/pdb
Descriptor	N-alpha-acetyltransferase, ACETYL COENZYME *A, CALCIUM ION, ... (4 entities in total)
Functional Keywords	acetyltransferase, transferase
Biological source	Sulfolobus solfataricus P2
Total number of polymer chains	1
Total formula weight	21362.37
Authors	Chang, Y.Y.,Hsu, C.H. (deposition date: 2018-08-09, release date: 2019-08-14, Last modification date: 2023-11-22)
Primary citation	Chang, Y.Y.,Hagawa, S.,Hsu, C.H. Adaptation of thermophilic acetyltransferase to a water-mediated catalytic mechanism. Chem.Commun.(Camb.), 56:10537-10540, 2020 Cited by PubMed Abstract: 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. PubMed: 32780067 DOI: 10.1039/d0cc04305b PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.32 Å)

Structure validation