4kay

Structure of the soluble domain of Lipooligosaccharide phosphoethanolamine transferase A from Neisseria meningitidis - complex with Zn

spinqualitylabelsall models 4kay, resolution 1.78Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4kay is a 2 chain structure with sequence from Neisseria meningitidis MC58. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.781Å Ligands: PO4, TPO, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q7DD94_NEIMB Publication Abstract from PubMed Gram-negative bacteria, possess an outer membrane envelope consisting of an outer leaflet of lipopolysaccharides (LPS), also called endotoxins, which protect the pathogen from antimicrobial peptides and have multi-faceted roles in virulence. LPS consists of a glycan moiety attached to Lipid A, embedded in the outer membrane. Modification of the lipid A headgroups by phosphoethanolamine or 4-amino-arabinose residues increase resistance to the cationic cyclic polypeptide antibiotic, polymyxin. Lipid A phosphoethanolamine transferases are members of the YhjW/YjdB/YijP superfamily and usually consist of a transmembrane domain anchoring the enzyme to the periplasmic face of the cytoplasmic membrane attached to a soluble catalytic domain. In order to understand the catalytic mechanism of lipid A modification by this enzyme the crystal structure of the soluble domain of the protein of the lipid A phosphoethanolamine transferase (LptA) from Neisseria meningitidis has been determined crystallographically and refined to 1.4A resolution. The structure reveals a core hydrolase fold similar to that of alkaline phosphatase. Loop regions in the structure differ, presumably to enable interaction with the membrane localised substrates and to provide substrate specificity. A phosphorylated form of the putative nucleophile, Thr280, is observed. Metal ions present in the active site are coordinated to Thr280 and to residues conserved amongst the family of transferases. The structure reveals the protein components needed for the transferase chemistry however substrate-binding regions are not evident and are likely to reside in the transmembrane domain of the protein. The structure of the Neisserial Lipooligosaccharide phosphoethanolamine transferase A (LptA) required for resistance to polymyxin.,Wanty C, Anandan A, Piek S, Walshe J, Ganguly J, Carlson RW, Stubbs KA, Kahler CM, Vrielink A J Mol Biol. 2013 Jun 27. pii: S0022-2836(13)00423-3. doi:, 10.1016/j.jmb.2013.06.029. PMID:23810904 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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