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Literature summary for 2.3.1.191 extracted from

  • Buetow, L.; Smith, T.K.; Dawson, A.; Fyffe, S.; Hunter, W.N.
    Structure and reactivity of LpxD, the N-acyltransferase of lipid A biosynthesis (2007), Proc. Natl. Acad. Sci. USA, 104, 4321-4326.
    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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 Chlamydia trachomatis

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapor diffusion. Crystallographic analyses of recombinant Chlamydia trachomatis LpxD in complex with UDP-GlcNAc, which represents a fragment of substrate, and fatty acid extracted from the bacterial expression system, apo-structure at 2.7 A resolution, and two structures with bound UDP-N-acetylglucosamine (UDP-GlcNAc) at 2.2 A and 3.1 A resolution Chlamydia trachomatis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(3R)-3-hydroxyarachidonoyl-[acyl-carrier protein] + UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine Chlamydia trachomatis the external layer of the Gram-negative bacterial outer membrane is primarily composed of a protective, selectively permeable lipopolysaccharide. The biosynthesis of lipopolysaccharide relies on UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD), which transfers 3-hydroxy-arachidonic acid from acyl carrier protein to the 2' amine of UDP-3-O-myristoyl glucosamine. CtLpxD is expected to utilize R-3-hydroxyarachidonoyl-[acyl-carrier protein] and UDP-3-O-(myristoyl)-R-D-glucosamine, based on the predominant molecular species of Chlamydia trachomatis lipid A. This proposal is not validated by in vitro assays UDP-2-N-((3R)-3-hydroxyarachidonoyl)-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine + holo-[acyl-carrier protein]
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Organism

Organism UniProt Comment Textmining
Chlamydia trachomatis P0CD76
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Purification (Commentary)

Purification (Comment) Organism
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 Chlamydia trachomatis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(3R)-3-hydroxyarachidonoyl-[acyl-carrier protein] + UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine the external layer of the Gram-negative bacterial outer membrane is primarily composed of a protective, selectively permeable lipopolysaccharide. The biosynthesis of lipopolysaccharide relies on UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD), which transfers 3-hydroxy-arachidonic acid from acyl carrier protein to the 2' amine of UDP-3-O-myristoyl glucosamine. CtLpxD is expected to utilize R-3-hydroxyarachidonoyl-[acyl-carrier protein] and UDP-3-O-(myristoyl)-R-D-glucosamine, based on the predominant molecular species of Chlamydia trachomatis lipid A. This proposal is not validated by in vitro assays Chlamydia trachomatis UDP-2-N-((3R)-3-hydroxyarachidonoyl)-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine + holo-[acyl-carrier protein]
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 ?
additional information His247 and His284 contribute to a mechanism involving nucleophilic attack by the amine of one substrate on the carbonyl carbon of an acyl carrier protein thioester conjugate Chlamydia trachomatis ?
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Subunits

Subunits Comment Organism
homotrimer each subunit of which is constructed from a novel combination of an N-terminal uridine binding domain, a core lipid-binding domain, and a C-terminal helical extension. Highly conserved residues dominate nucleotide binding. Phe43 and Tyr49 form pi-stacking interactions with uracil, and Asn46 and His284 form hydrogen bonds with the phosphate groups Chlamydia trachomatis

Synonyms

Synonyms Comment Organism
CtLpxD
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 Chlamydia trachomatis
UDP-3-O-acyl-glucosamine N-acyltransferase
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 Chlamydia trachomatis