4e79 | pdb_00004e79

Structure of LpxD from Acinetobacter baumannii at 2.66A resolution (P4322 form)

spinqualitylabelsall models 4e79, resolution 2.66Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4e79 is a 3 chain structure with sequence from Acinetobacter baumannii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [LPXD_ACIBS] Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.[HAMAP-Rule:MF_00523] Publication Abstract from PubMed 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 A 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. Structure determination of LpxD from the lipopolysaccharide-synthesis pathway of Acinetobacter baumannii.,Badger J, Chie-Leon B, Logan C, Sridhar V, Sankaran B, Zwart PH, Nienaber V Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Jan 1;69(Pt 1):6-9. doi:, 10.1107/S1744309112048890. Epub 2012 Dec 25. PMID:23295477 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase

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