Literature summary for 2.3.1.129 extracted from

Smith, E.W.; Zhang, X.; Behzadi, C.; Andrews, L.D.; Cohen, F.; Chen, Y.
Structures of Pseudomonas aeruginosa LpxA reveal the basis for its substrate selectivity (2015), Biochemistry, 54, 5937-5948.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
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	Pseudomonas aeruginosa

Crystallization (Comment)

Organism

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

Pseudomonas aeruginosa

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas aeruginosa	A6V1E4	-	-
Pseudomonas aeruginosa PA7	A6V1E4	-	-

Synonyms

Synonyms	Comment	Organism
LpxA	-	Pseudomonas aeruginosa

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Release 2023.1 (January 2023)