v5.1.0.3
Glycine data from LIS
Type | Repeat |
Description | 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 (Acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase) [ ], has been shown to form a left-handed parallel β-helix. A number of different transferase protein families contain this repeat, such as the bifunctional protein GlmU, galactoside acetyltransferase-like proteins [], the gamma-class of carbonic anhydrases [], and tetrahydrodipicolinate-N-succinlytransferases (DapD), the latter containing an extra N-terminal 3-helical domain []. It has been shown that most hexapeptide acyltransferases form catalytic trimers with three symmetrical active sites []. |
Short Name | Hexapep |