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Literature summary for 2.3.1.191 extracted from

  • Masoudi, A.; Raetz, C.R.; Zhou, P.; Pemble, C.W.
    Chasing acyl carrier protein through a catalytic cycle of lipid A production (2014), Nature, 505, 422-426.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.3.1.191

Cloned(Commentary)

Cloned (Comment) Organism
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 Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
in complex with three forms of acyl carrier protein. Interactions at the interface optimally position acyl carrier protein for acyl delivery and directly involve the pantetheinyl group Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P21645
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information ordered-sequential reaction mechanism. Acyl-ACP binds first to free LpxD forming a binary complex. ACP associates with the ACP-recognition domain and the acyl-4'-phosphopantetheine group packs into the hydrophobic N-channel. UDP-acyl-GlcN binds next, which initiates acyl transfer. In the ternary product complex, the 4'-phosphopantetheine arm of hydrolysed-acyl-ACP completely encloses the reaction chamber, blocking UDP-diacyl-GlcN from leaving. By moving the 4'-phosphopantetheine group towards Met 290, the catalytic chamber opens up. This motion drives the eventual release of UDP-diacyl-GlcN and triggers conformational changes downstream of helix-II leading to holo-ACP dissociation Escherichia coli ?
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