4E75

Structure of LpxD from Acinetobacter baumannii at 2.85A resolution (P21 form)

Summary for 4E75

• Entry DOI: 10.2210/pdb4e75/pdb
• Related: 4E6T 4E6U 4E79
• Descriptor: UDP-3-O-acylglucosamine N-acyltransferase (1 entity in total)
• Functional Keywords: lipopolysaccaride synthesis, transferase
• Biological source: Acinetobacter baumannii
• Total number of polymer chains: 6
• Total formula weight: 230834.90

Authors

Badger, J.,Chie-Leon, B.,Logan, C.,Sridhar, V.,Sankaran, B.,Zwart, P.H.,Nienaber, V. (deposition date: 2012-03-16, release date: 2013-01-16, Last modification date: 2023-09-13)

Primary citation

Badger, J.,Chie-Leon, B.,Logan, C.,Sridhar, V.,Sankaran, B.,Zwart, P.H.,Nienaber, V.
Structure determination of LpxD from the lipopolysaccharide-synthesis pathway of Acinetobacter baumannii.
Acta Crystallogr.,Sect.F, 69:6-9, 2013

PubMed Abstract: Acinetobacter baumannii is a Gram-negative bacterium that is resistant to many currently available antibiotics. The protein LpxD is a component of the biosynthetic pathway for lipopolysaccharides in the outer membrane of this bacterium and is a potential target for new antibacterial agents. This paper describes the structure determination of apo forms of LpxD in space groups P2(1) and P4(3)22. These crystals contained six and three copies of the protein molecule in the asymmetric unit and diffracted to 2.8 and 2.7 Å resolution, respectively. A comparison of the multiple protein copies in the asymmetric units of these crystals reveals a common protein conformation and a conformation in which the relative orientation between the two major domains in the protein is altered.

PubMed: 23295477
DOI: 10.1107/S1744309112048890

Experimental method

X-RAY DIFFRACTION (2.85 Å)