Member database | PROSITE profiles |
PROSITE profiles type | domain |
Short name | GNAT_ATAT |
Description
References
1.GCN5-related N-acetyltransferases: a structural overview. Dyda F, Klein DC, Hickman AB. 29, 81-103, (2000). View articlePMID: 10940244
2.Crystal structures of tubulin acetyltransferase reveal a conserved catalytic core and the plasticity of the essential N terminus. Kormendi V, Szyk A, Piszczek G, Roll-Mecak A. J. Biol. Chem. 287, 41569-75, (2012). View articlePMID: 23105108
3.Crystal structure of tabtoxin resistance protein complexed with acetyl coenzyme A reveals the mechanism for beta-lactam acetylation. He H, Ding Y, Bartlam M, Sun F, Le Y, Qin X, Tang H, Zhang R, Joachimiak A, Liu J, Zhao N, Rao Z. J. Mol. Biol. 325, 1019-30, (2003). View articlePMID: 12527305
4.X-ray structure of the AAC(6')-Ii antibiotic resistance enzyme at 1.8 A resolution; examination of oligomeric arrangements in GNAT superfamily members. Burk DL, Ghuman N, Wybenga-Groot LE, Berghuis AM. Protein Sci. 12, 426-37, (2003). View articlePMID: 12592013
5.Structure and functions of the GNAT superfamily of acetyltransferases. Vetting MW, S de Carvalho LP, Yu M, Hegde SS, Magnet S, Roderick SL, Blanchard JS. Arch. Biochem. Biophys. 433, 212-26, (2005). View articlePMID: 15581578
6.Crystal structure of the N-acetyltransferase domain of human N-acetyl-L-glutamate synthase in complex with N-acetyl-L-glutamate provides insights into its catalytic and regulatory mechanisms. Zhao G, Jin Z, Allewell NM, Tuchman M, Shi D. PLoS ONE 8, e70369, (2013). View articlePMID: 23894642
7.Structure of an acetyl-CoA binding protein from Staphylococcus aureus representing a novel subfamily of GCN5-related N-acetyltransferase-like proteins. Cort JR, Ramelot TA, Murray D, Acton TB, Ma LC, Xiao R, Montelione GT, Kennedy MA. J. Struct. Funct. Genomics 9, 7-20, (2008). View articlePMID: 18709443
8.GCN5-related histone N-acetyltransferases belong to a diverse superfamily that includes the yeast SPT10 protein. Neuwald AF, Landsman D. Trends Biochem. Sci. 22, 154-5, (1997). View articlePMID: 9175471