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Literature summary for 3.5.1.108 extracted from

  • Buetow, L.; Dawson, A.; Hunter, W.N.
    The nucleotide-binding site of Aquifex aeolicus LpxC (2006), Acta Crystallogr. Sect. F, 62, 1082-1086.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
crystals of LpxC are grown by hanging-drop vapour diffusion at 20°C, structure of recombinant UDP-3-O-acyl-N-acetylglucosamine deacetylase in complex with UDP, determined to a resolution of 2.2 A. The uracil-binding site is constructed from amino acids that are highly conserved across species. Hydrophobic associations with the Phe155 and Arg250 side chains in combination with hydrogen-bonding interactions with the main chain of Glu154 and the side chains of Tyr151 and Lys227 position the base. The phosphate and ribose groups are directed away from the active site and interact with Arg137, Lys156, Glu186 and Arg250 Aquifex aeolicus

Organism

Organism UniProt Comment Textmining
Aquifex aeolicus O67648
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Synonyms

Synonyms Comment Organism
UDP-3-O-acyl-N-acetylglucosamine deacetylase
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Aquifex aeolicus