5k8k
From Proteopedia
Jump to navigationJump to search
Structure of the Haemophilus influenzae LpxH-lipid X complex
| ||||||||||||
Structural highlights
FunctionLPXH_HAEIN Catalyzes the hydrolysis of the pyrophosphate bond of UDP-2,3-diacylglucosamine to yield 2,3-diacylglucosamine 1-phosphate (lipid X) and UMP. Publication Abstract from PubMedIn 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. Structure of the essential Haemophilus influenzae UDP-diacylglucosamine pyrophosphohydrolase LpxH in lipid A biosynthesis.,Cho J, Lee CJ, Zhao J, Young HE, Zhou P Nat Microbiol. 2016 Aug 15;1(11):16154. doi: 10.1038/nmicrobiol.2016.154. PMID:27780190[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||||
This page was last modified 10:43, 27 September 2023.