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Space-filling views of the region containing the N-terminal tag sequence in the structure from P. aeruginosa (right) and UDP-GlcNac binding in a structure from C. trachomatis (PDB entry 2iu8, left)
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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.
Acta Crystallographica Section F – Wiley
Published: Jul 1, 2011
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