1LXA

UDP N-ACETYLGLUCOSAMINE ACYLTRANSFERASE

Summary for 1LXA

• Entry DOI: 10.2210/pdb1lxa/pdb
• Descriptor: UDP N-ACETYLGLUCOSAMINE O-ACYLTRANSFERASE (1 entity in total)
• Functional Keywords: transferase, acyltransferase, lipid a biosynthesis, lipid synthesis
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 28117.02

Authors

Roderick, S.L. (deposition date: 1995-10-07, release date: 1995-12-07, Last modification date: 2024-02-14)

Primary citation

Raetz, C.R.,Roderick, S.L.
A left-handed parallel beta helix in the structure of UDP-N-acetylglucosamine acyltransferase.
Science, 270:997-1000, 1995

PubMed Abstract: UDP-N-acetylglucosamine 3-O-acyltransferase (LpxA) catalyzes the transfer of (R)-3-hydroxymyristic acid from its acyl carrier protein thioester to UDP-N-acetylglucosamine. LpxA is the first enzyme in the lipid A biosynthetic pathway and is a target for the design of antibiotics. The x-ray crystal structure of LpxA has been determined to 2.6 angstrom resolution and reveals a domain motif composed of parallel beta strands, termed a left-handed parallel beta helix (L beta H). This unusual fold displays repeated violations of the protein folding constraint requiring right-handed crossover connections between strands of parallel beta sheets and may be present in other enzymes that share amino acid sequence homology to the repeated hexapeptide motif of LpxA.

PubMed: 7481807

Experimental method

X-RAY DIFFRACTION (2.6 Å)