R
IPR001451

Hexapeptide repeat

InterPro entry
Short nameHexapep
Overlapping
homologous
superfamilies
 

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)
[1]
, 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
[4]
, the gamma-class of carbonic anhydrases
[2]
, and tetrahydrodipicolinate-N-succinlytransferases (DapD), the latter containing an extra N-terminal 3-helical domain
[3]
. It has been shown that most hexapeptide acyltransferases form catalytic trimers with three symmetrical active sites
[5]
.

References

1.A left-handed parallel beta helix in the structure of UDP-N-acetylglucosamine acyltransferase. Raetz CR, Roderick SL. Science 270, 997-1000, (1995). View articlePMID: 7481807

2.A closer look at the active site of gamma-class carbonic anhydrases: high-resolution crystallographic studies of the carbonic anhydrase from Methanosarcina thermophila. Iverson TM, Alber BE, Kisker C, Ferry JG, Rees DC. Biochemistry 39, 9222-31, (2000). View articlePMID: 10924115

3.Acyl group specificity at the active site of tetrahydridipicolinate N-succinyltransferase. Beaman TW, Vogel KW, Drueckhammer DG, Blanchard JS, Roderick SL. Protein Sci. 11, 974-9, (2002). View articlePMID: 11910040

4.Structure of the lac operon galactoside acetyltransferase. Wang XG, Olsen LR, Roderick SL. Structure 10, 581-8, (2002). View articlePMID: 11937062

5.Biochemical characterization of the polysialic acid-specific O-acetyltransferase NeuO of Escherichia coli K1. Bergfeld AK, Claus H, Vogel U, Muhlenhoff M. J. Biol. Chem. 282, 22217-27, (2007). PMID: 17519228

Cross References

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