5K8K
Structure of the Haemophilus influenzae LpxH-lipid X complex
Summary for 5K8K
| Entry DOI | 10.2210/pdb5k8k/pdb |
| Descriptor | UDP-2,3-diacylglucosamine hydrolase, MANGANESE (II) ION, (R)-((2R,3S,4R,5R,6R)-3-HYDROXY-2-(HYDROXYMETHYL)-5-((R)-3-HYDROXYTETRADECANAMIDO)-6-(PHOSPHONOOXY)TETRAHYDRO-2H-PYRAN-4-YL) 3-HYDROXYTETRADECANOATE, ... (6 entities in total) |
| Functional Keywords | lpxh, lipid x, udp-diacylglucosamine, lipid a, lps, lipopolysaccharide, antibiotic, calcineurin-like phosphoesterase, hydrolase |
| Biological source | Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) |
| Total number of polymer chains | 1 |
| Total formula weight | 31639.98 |
| Authors | Cho, J.,Lee, C.-J.,Zhou, P. (deposition date: 2016-05-30, release date: 2016-08-10, Last modification date: 2024-10-23) |
| Primary citation | Cho, J.,Lee, C.J.,Zhao, J.,Young, H.E.,Zhou, P. Structure of the essential Haemophilus influenzae UDP-diacylglucosamine pyrophosphohydrolase LpxH in lipid A biosynthesis. Nat Microbiol, 1:16154-16154, 2016 Cited by PubMed 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. PubMed: 27780190DOI: 10.1038/nmicrobiol.2016.154 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.55 Å) |
Structure validation
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