Literature summary for 2.3.1.129 extracted from

Jenkins, R.J.; Heslip, K.A.; Meagher, J.L.; Stuckey, J.A.; Dotson, G.D.
Structural basis for the recognition of peptide RJPXD33 by acyltransferases in lipid A biosynthesis (2014), J. Biol. Chem., 289, 15527-15535.

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
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	Escherichia coli

Crystallization (Comment)

Organism

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

Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0A722	-	-

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Release 2023.1 (January 2023)