InterPro domain: IPR001451

A variety of bacterial transferases contain a repeat structure composed of tandem repeats of a [LIV]-G-X(4) hexapeptide, which, in the tertiary structure of LpxA (UDP N-acetylglucosamine acyltransferase) [ 1 ], has been shown to form a left-handed parallel beta helix. A number of different transferase protein families contain this repeat, such as galactoside acetyltransferase-like proteins [ 2 ], the gamma-class of carbonic anhydrases [ 3 ], and tetrahydrodipicolinate-N-succinlytransferases (DapD), the latter containing an extra N-terminal 3-helical domain [ 4 ]. It has been shown that most hexapeptide acyltransferases form catalytic trimers with three symmetrical active sites [ 5 ].

1. A left-handed parallel beta helix in the structure of UDP-N-acetylglucosamine acyltransferase. Science 270, 997-1000
2. Structure of the lac operon galactoside acetyltransferase. Structure 10, 581-8
3. A closer look at the active site of gamma-class carbonic anhydrases: high-resolution crystallographic studies of the carbonic anhydrase from Methanosarcina thermophila. Biochemistry 39, 9222-31
4. Acyl group specificity at the active site of tetrahydridipicolinate N-succinyltransferase. Protein Sci. 11, 974-9
5. Biochemical characterization of the polysialic acid-specific O-acetyltransferase NeuO of Escherichia coli K1. J. Biol. Chem. 282, 22217-27