3PMO

The structure of LpxD from Pseudomonas aeruginosa at 1.3 A resolution

Summary for 3PMO

• Entry DOI: 10.2210/pdb3pmo/pdb
• Descriptor: UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase, 1,2-ETHANEDIOL, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: lipid a biosynthesis pathway, transferase
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 1
• Total formula weight: 38425.77

Authors

Badger, J.,Chie-Leon, B.,Logan, C.,Sridhar, V.,Sankaran, B.,Zwart, P.H.,Nienaber, V. (deposition date: 2010-11-17, release date: 2011-07-27, Last modification date: 2024-02-21)

Primary citation

Badger, J.,Chie-Leon, B.,Logan, C.,Sridhar, V.,Sankaran, B.,Zwart, P.H.,Nienaber, V.
The structure of LpxD from Pseudomonas aeruginosa at 1.3 A resolution.
Acta Crystallogr.,Sect.F, 67:749-752, 2011

PubMed 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.

PubMed: 21795786
DOI: 10.1107/S1744309111018811

Experimental method

X-RAY DIFFRACTION (1.3 Å)