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2.3.1.129: acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase

This is an abbreviated version!
For detailed information about acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase, go to the full flat file.

Word Map on EC 2.3.1.129

Reaction

a (3R)-3-hydroxyacyl-[acyl-carrier protein]
+
UDP-N-acetyl-alpha-D-glucosamine
=
an [acyl-carrier protein]
 +
a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine

Synonyms

acyltransferase, uridine diphosphoacetylglucosamine, LiLpxA, LpxA, type II ACP-dependent UDP-N-acetylglucosamine acyltransferase, type II acyl carrier protein-dependent UDP-N-acetylglucosamine acyltransferase, UDP-N-acetylglucosamine 3-O-acyltransferase, UDP-N-acetylglucosamine acyltransferase, uridine diphosphoacetylglucosamine acyltransferase

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.129 acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase

Crystallization

Crystallization on EC 2.3.1.129 - acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant LpxA, sitting drop vapor diffusion method, mixing of AtLpxA at 18 mg/mL in 10 mM potassium phosphate buffer, pH 7.0, 200 mM KCl, and 20% glycerol, in a 1:1 ratio with precipitant solution containing 0.5 M ammonium sulfate, 0.1 M sodium citrate, pH 5.6, and 1.0 M lithium sulfate monohydrate, equilibration at 20°C, 1-2 days, X-ray diffraction structure determination and analysis at 2.1 A resolution
structures of ligand-free and UDP-GlcNAc-bound enzyme. The enzyme crystallizes in a cubic space group, with the crystallographic threefold axis generating the biological functional homotrimer and with each monomer forming a nine-ring left-handed beta-helical fold in the N-terminus followed by an alpha-helical motif in the C-terminus. Calcium ions are observed on the threefold axis to help stabilize the trimeric assembly
by the sitting-drop, vapour-diffusion method using 0.00l ml of protein solution
by using the hanging drop vapor diffusion method, in the presence of a 25-fold molar excess of either UDP-3-O-(R-3-hydroxymyristoyl)-GlcNAc or UDP-3-O-(R-3-hydroxydecanoyl)-GlcNAc, structures show how LpxA selects for 14-carbon R-3-hydroxyacyl chains and reveal two modes of UDP binding
in complex with inhibitor peptide WMLDPIAGKWSR, to 1.6 A resolution. The peptide is located at the interface of each adjacent subunit and interacts with residues from both sides. It occupies part of the ACP binding site
LpxA in complex with UDP-GlcNAc, modelling
purified enzyme LpxA in a complex with inhibitor peptide 920, 20 mg/ml protein in solution with a 25fold molar excess of peptide 920 of 12.5 mM, crystal growth at 18°C, hanging drop vapor diffusion method, mixing of 0.002 ml protein solution with 0.002 ml of 0.8–1.8 M phosphate buffer, pH 6.3–6.9, and 30-35% DMSO, about 2 weeks, X-ray diffraction structure determination and analysis at 1.8 A resolution, molecular replacement using crystal structure PDB ID code 1LXA, determined at 2.6 A resolution
structure in complex with peptide RJPXD33 at 1.9 A resolution. Results suggest that the peptide binds in a unique modality that mimics (R)-beta-hydroxyacyl pantetheine binding to LpxA. REsidue H160 changes its conformation upon binding of peptide. Overlay of the LpxA RJPXD33 structure with LpxD, EC 2.31.191, identifies a complementary peptide binding pocket within LpxD and serves as a model for characterization of RJPXD33 binding to LpxD
structure to 2.06 A resolution. The supposed ruler residues for hydrocarbon length, L171 in one monomer and H168 in the adjacent monomer in a functional trimer of LpxA, are located just 3.8 A apart that renders not enough space for binding of 3-OH-laurate or longer acyl chains
-
crystallized at 297 K using (NH4)2SO4 and Na/K tartrate as precipitants in the presence of a detergent, space group: P6322 with unit cell-parameters: a = b = 90.69, and c = 148.20 ANG
-
purified recombinant, C-terminally eight-residue-tagged enzyme, X-ray diffraction structure analysis at 2.1 A resolution, modeling of the enzyme complexed with [acyl-carrier protein]
-
crystal structures of free LiLpxA and its complexes with its product UDP-3-N-((R)-3-hydroxylauroyl)-GlcNAc3N and with its substrate (R)-3-hydroxylauroyl-methylphosphopantetheine are presented. The selectivity of LiLpxA for UDPGlcNAc3N may be explained by the orientation of the backbone carbonyl group of Q68, which differs by 82° from the corresponding Q73 carbonyl group in Escherichia coli LpxA. This arrangement provides an extra hydrogen-bond acceptor for the 3-NH2 group of UDP-GlcNAc3N in LiLpxA. The R-3-hydroxylauroyl selectivity of LiLpxA is explained by the position of the K171 side chain, which limits the length of the acyl-chain-binding groove. H120 functions as a catalytic base
the residues D69, L70, K71, H117, H120,G138, H139, Q156 from one chain and N193, R199 from the adjacent chain form the active site and play crucial role in substrate positioningand catalysis
structures of apo protein, substrate complex with UDP-GlcNAc, and product complex with UDP-3-O-(R-3-hydroxydecanoyl)-GlcNAc. Catalytic His121 is involved in activating the UDP-GlcNAc 3-hydroxyl group for nucleophilic attack during the reaction. Met169 serves to constrain the length of the acyl chain and thus functions as the so-called hydrocarbon ruler. The purported oxyanion hole, formed by the backbone amide group of Gly139, displays a different conformation in Pseudomonas aeruginosa LpxA, which suggests flexibility of this structural feature important for catalysis and the potential need for substrate-induced conformational change in catalysis