2.7.8.43	?	x * 36700, recombinant His-tagged wild-type, SDS-PAGE	-, 739786	
2.7.8.43	?	x * 60000, about, sequence calculation	-, 739495	
2.7.8.43	additional information	according to light scattering data, LptA oligomerizes in a concentration-dependent manner. LptA is an average of a trimer in solution, and a considerably higher order oligomerization state (25mers) is predicted at a protein concentration of 0.1 mM	752134	
2.7.8.43	additional information	enzyme structure analysis, overview	-, 739786	
2.7.8.43	additional information	secondary-structure ribbon representation of the soluble domain of LptA, and modeling of the three-dimensional structure of LptA, overview. Possible formation of five intramolecular disulfide bonds: Cys276-Cys286, Cys327-Cys331, Cys348-Cys353, Cys402-Cys410, and Cys499-Cys540	-, 734476	
2.7.8.43	additional information	the enzyme is composed of an N-terminal transmembrane domain and a C-terminal soluble domain. Tryptic peptide mapping and analysis by MALDI-TOF/TOF mass spectrometry	-, 733017	
2.7.8.43	oligomer	the enzyme LptA arranges in an end-to-end fibrous tetramer, which forms a continuous hydrophobic groove between the LptA monomers, crystal structure analysis. Mass spectral analysis confirmes that LptA forms 2-5-member oligomers in a concentration-dependent manner when purified in vitro and that the resultant complexes are stabilized by LPS. Analysis of subunit interactions	750867