ArticleBiochemistry2009
Structural basis for the sugar nucleotide and acyl-chain selectivity of Leptospira interrogans LpxA.
Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Plant cell wall architecture guided design of CBM3-GH11 chimeras with enhanced xylanase activity using a tandem repeat left-handed β-3-prism scaffold.Computational and structural biotechnology journal · 2021Article
- Structure-Based Virtual Screening ofBiomolecules · 2020Article
- Structure guided design of an antibacterial peptide that targets UDP-N-acetylglucosamine acyltransferase.Scientific reports · 2019Article
- Network-Based Metabolism-Centered Screening of Potential Drug Targets inFrontiers in cellular and infection microbiology · 2019Article
- Article
- Structure, inhibition, and regulation of essential lipid A enzymes.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2017Review
- Crystal structure and activity of Francisella novicida UDP-N-acetylglucosamine acyltransferase.Biochemical and biophysical research communications · 2016Article
- Article
- Lipid A as a Drug Target and Therapeutic Molecule.Biomolecules & therapeutics · 2015Review
- Structures of Bacteroides fragilis uridine 5'-diphosphate-N-acetylglucosamine (UDP-GlcNAc) acyltransferase (BfLpxA).Acta crystallographica. Section D, Biological crystallography · 2015Article
- Structural basis for the recognition of peptide RJPXD33 by acyltransferases in lipid A biosynthesis.The Journal of biological chemistry · 2014Article
- Acyltransferases in bacteria.Microbiology and molecular biology reviews : MMBR · 2013Review
- Structure determination of LpxA from the lipopolysaccharide-synthesis pathway of Acinetobacter baumannii.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
- LpxI structures reveal how a lipid A precursor is synthesized.Nature structural & molecular biology · 2012Article
- Activity and crystal structure of Arabidopsis thaliana UDP-N-acetylglucosamine acyltransferase.Biochemistry · 2012Article
- The Raetz pathway for lipid A biosynthesis: Christian Rudolf Hubert Raetz, MD PhD, 1946–2011.Journal of lipid research · 2011Article
- Species-specific and inhibitor-dependent conformations of LpxC: implications for antibiotic design.Chemistry & biology · 2011Article
- Crystal structure and acyl chain selectivity of Escherichia coli LpxD, the N-acyltransferase of lipid A biosynthesis.Biochemistry · 2009Article
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3 authors.
Funding
Abstract
The first step of lipid A biosynthesis is catalyzed by LpxA in Escherichia coli (EcLpxA), an acyltransferase selective for UDP-GlcNAc and R-3-hydroxymyristoyl-acyl carrier protein (ACP). Leptospira interrogans LpxA (LiLpxA) is extremely selective for R-3-hydroxylauroyl-ACP and an analogue of UDP-GlcNAc, designated UDP-GlcNAc3N, in which NH(2) replaces the GlcNAc 3-OH group. EcLpxA does not discriminate between UDP-GlcNAc and UDP-GlcNAc3N; however, E. coli does not make UDP-GlcNAc3N. With LiLpxA, R-3-hydroxylauroyl-methylphosphopantetheine efficiently substitutes for R-3-hydroxylauroyl-ACP. We now present crystal structures of free LiLpxA and its complexes with its product UDP-3-N-(R-3-hydroxylauroyl)-GlcNAc3N and with its substrate R-3-hydroxylauroyl-methylphosphopantetheine. The positions of the acyl chains of the R-3-hydroxylauroyl-methylphosphopantetheine and the UDP-3-N-(R-3-hydroxylauroyl)-GlcNAc3N are almost identical and are similar to that of the acyl chain in the EcLpxA/UDP-3-O-(R-3-hydroxymyristoyl)-GlcNAc complex. The selectivity of LiLpxA for UDP-GlcNAc3N may be explained by the orientation of the backbone carbonyl group of Q68, which differs by approximately 82 degrees from the corresponding Q73 carbonyl group in EcLpxA. This arrangement provides an extra hydrogen-bond acceptor for the 3-NH(2) group of UDP-GlcNAc3N in LiLpxA. The R-3-hydroxylauroyl selectivity of LiLpxA is explained by the position of the K171 side chain, which limits the length of the acyl-chain-binding groove. Our results support the role of LiLpxA H120 (which corresponds to EcLpxA H125) as the catalytic base and provide the first structural information about the orientation of the phosphopantetheine moiety during LpxA catalysis.
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