4E6U

Structure of LpxA from Acinetobacter baumannii at 1.4A resolution (P63 form)

Summary for 4E6U

• Entry DOI: 10.2210/pdb4e6u/pdb
• Related: 4E6T 4E75 4E79
• Descriptor: Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase, SULFATE ION, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: lipopolysaccaride synthesis, transferase
• Biological source: Acinetobacter baumannii
• Cellular location: Cytoplasm (By similarity): F0QHB3
• Total number of polymer chains: 1
• Total formula weight: 29223.07

Authors

Badger, J.,Chie-Leon, B.,Logan, C.,Sridhar, V.,Sankaran, B.,Zwart, P.H.,Nienaber, V. (deposition date: 2012-03-16, release date: 2012-12-12, Last modification date: 2024-02-28)

Primary citation

Badger, J.,Chie-Leon, B.,Logan, C.,Sridhar, V.,Sankaran, B.,Zwart, P.H.,Nienaber, V.
Structure determination of LpxA from the lipopolysaccharide-synthesis pathway of Acinetobacter baumannii.
Acta Crystallogr.,Sect.F, 68:1477-1481, 2012

PubMed Abstract: Acinetobacter baumannii is a Gram-negative pathogenic bacterium which is resistant to most currently available antibiotics and that poses a significant health threat to hospital patients. LpxA is a key enzyme in the biosynthetic pathway of the lipopolysaccharides that are components of the bacterial outer membrane. It is a potential target for antibacterial agents that might be used to fight A. baumannii infections. This paper describes the structure determination of the apo form of LpxA in space groups P2(1)2(1)2(1) and P6(3). These crystal forms contained three and one protein molecules in the asymmetric unit and diffracted to 1.8 and 1.4 Å resolution, respectively. A comparison of the conformations of the independent protein monomers within and between the two crystal asymmetric units revealed very little structural variation across this set of structures. In the P6(3) crystal form the enzymatic site is exposed and is available for the introduction of small molecules of the type used in fragment-based drug discovery and structure-based lead optimization.

PubMed: 23192027
DOI: 10.1107/S174430911204571X

Experimental method

X-RAY DIFFRACTION (1.41 Å)