title: Structure of the essential Haemophilus influenzae UDP-diacylglucosamine pyrophosphohydrolase LpxH in lipid A biosynthesis.
abstract: 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.
authors: Department of Biochemistry, Duke University Medical Center, Research Drive, Durham, North Carolina 27710, USA.
authors: Jae
authors: J
authors: Cho
authors: Department of Biochemistry, Duke University Medical Center, Research Drive, Durham, North Carolina 27710, USA.
authors: Chul-Jin
authors: CJ
authors: Lee
authors: Department of Biochemistry, Duke University Medical Center, Research Drive, Durham, North Carolina 27710, USA.
authors: Jinshi
authors: J
authors: Zhao
authors: Department of Biochemistry, Duke University Medical Center, Research Drive, Durham, North Carolina 27710, USA.
authors: Hayley E
authors: HE
authors: Young
authors: Department of Biochemistry, Duke University Medical Center, Research Drive, Durham, North Carolina 27710, USA.
authors: Pei
authors: P
authors: Zhou
mesh_terms: D055162:Biocatalysis; D050260:Carbohydrate Metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D006017:Glycolipids / Q000737:chemistry*; D006193:Haemophilus influenzae / Q000201:enzymology* / Q000378:metabolism; D006868:Hydrolysis; D008050:Lipid A / Q000096:biosynthesis*; D008958:Models, Molecular; D011755:Pyrophosphatases / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D006017:Glycolipids; D008050:Lipid A; C044283:lipid X; D011755:Pyrophosphatases