In most Gram-negative pathogens, the hydrolysis of UDP-2,3-diacylglucosamine to generate lipid X in lipid A biosynthesis is catalysed by the membrane-associated enzyme LpxH. We report the crystal structure of LpxH in complex with its product, lipid X, unveiling a unique insertion lid above the conserved architecture of calcineurin-like phosphoesterases. This structure reveals elaborate interactions surrounding lipid X and provides molecular insights into the substrate selectivity, catalysis and inhibition of LpxH.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5081216PMC
http://dx.doi.org/10.1038/nmicrobiol.2016.154DOI Listing

Publication Analysis

Top Keywords

lipid biosynthesis
8
lipid
5
structure essential
4
essential haemophilus
4
haemophilus influenzae
4
influenzae udp-diacylglucosamine
4
udp-diacylglucosamine pyrophosphohydrolase
4
lpxh
4
pyrophosphohydrolase lpxh
4
lpxh lipid
4

Similar Publications

Arv1; a "Mover and Shaker" of Subcellular Lipids.

Contact (Thousand Oaks)

January 2025

Department of Biology, Barnard College at Columbia University, 3009 Broadway, New York, NY 10023, USA.

The composition of eukaryotic membranes reflects a varied but precise amalgam of lipids. The genetic underpinning of how such diversity is achieved or maintained is surprisingly obscure, despite its clear metabolic and pathophysiological impact. The Arv1 protein is represented in all eukaryotes and was initially identified in the model eukaryote as a candidate transporter of lipids from the endoplasmic reticulum.

View Article and Find Full Text PDF

Background: Oily skin not only threatens people with aesthetic and hygienic discomfort but also confronts them with annoying skin problems. To explore new skin care ingredients from herbal or plant extracts and understand their underlying mechanism for sebum control would assist in the discovery of desirable sebosuppressive agents, though it is still a deserving and challenging task.

Aim: To explore the effect of Camellia saponin (CS) on modulating the lipogenesis of human sebocytes.

View Article and Find Full Text PDF

Targeting IGF1 to alleviate obesity through regulating energy expenditure and fat deposition.

Sci China Life Sci

January 2025

State Key Laboratory of Pharmaceutical Biotechnology, Department of Endocrinology, Nanjing Drum Tower Hospital, The Affiliated Hospital of Nanjing University Medical School, Model Animal Research Center, Nanjing University, Nanjing, 210061, China.

Insulin-like growth factor 1 (IGF1) is a regulator of both cellular hypertrophy and lipogenesis, which are two key processes for pathogenesis of obesity. However, the in vivo role of IGF1 in the development of obesity remains unclear. Here, we show that IGF1 expression is increased in adipose tissue in obese human patients and animal models.

View Article and Find Full Text PDF

Arachidonate 15-lipoxygenase type B (ALOX15B) peroxidises polyunsaturated fatty acids to their corresponding fatty acid hydroperoxides, which are subsequently reduced into hydroxy-fatty acids. A dysregulated abundance of these biological lipid mediators has been reported in the skin and blood of psoriatic compared to healthy individuals. RNAscope and immunohistochemistry revealed increased ALOX15B expression in lesional psoriasis samples.

View Article and Find Full Text PDF

Background And Purpose: Perivascular adipose tissues (PVATs) play a critical role in modulating vascular homeostasis and protecting against cardiovascular dysfunction-mediated blood pressure dysregulation. We demonstrated that the activating transcription factor-3 (Atf3) gene in the PVAT is crucial for improving vascular wall tension abnormalities; however, its protective mechanism remains unclear. Herein, we aim to determine whether ATF3 regulates PVAT-derived relaxing factor (PVDRF) biosynthesis and if its secretion contributes to vasorelaxation.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!