title: The structure of LpxD from Pseudomonas aeruginosa at 1.3 Å resolution.
abstract: LpxD is a bacterial protein that is part of the biosynthesis pathway of lipid A and is responsible for transferring 3-hydroxymyristic acid from the R-3-hydroxymyristoyl-acyl carrier protein to the 2-OH group of UDP-3-O-(3-hydroxymyristoyl) glucosamine. The crystal structure of LpxD from Pseudomonas aeruginosa has been determined at high resolution (1.3 Å). The crystal belonged to space group H3, with unit-cell parameters a=b=106.19, c=93.38 Å, and contained one molecule in the asymmetric unit. The structure was solved by molecular replacement using the known structure of LpxD from Escherichia coli (PDB entry 3eh0) as a search model and was refined to Rwork=16.4% (Rfree=18.5%) using 91,655 reflections. The final protein model includes 355 amino-acid residues (including 16 amino acids from a 20 amino-acid N-terminal His tag), one chloride ion and two ethylene glycol molecules.
authors.affiliation: Zenobia Therapeutics, 505 Coast Boulevard South, Suite 111, La Jolla, CA 92122, USA. john@zenobiatherapeutics.com
authors.forename: John
authors.initials: J
authors.lastname: Badger
authors.forename: Barbara
authors.initials: B
authors.lastname: Chie-Leon
authors.forename: Cheyenne
authors.initials: C
authors.lastname: Logan
authors.forename: Vandana
authors.initials: V
authors.lastname: Sridhar
authors.forename: Banumathi
authors.initials: B
authors.lastname: Sankaran
authors.forename: Peter H
authors.initials: PH
authors.lastname: Zwart
authors.forename: Vicki
authors.initials: V
authors.lastname: Nienaber
mesh_terms: D000217:Acyltransferases / Q000737:chemistry*; D018360:Crystallography, X-Ray; D008024:Ligands; D008958:Models, Molecular; D020836:Protein Structure, Quaternary; D011550:Pseudomonas aeruginosa / Q000201:enzymology*; D040681:Structural Homology, Protein
chemical_list: D008024:Ligands; D000217:Acyltransferases