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Results 1 - 7 of 7
EC Number Subunits Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 2.7.8.43? x * 36700, recombinant His-tagged wild-type, SDS-PAGE -, 739786
Display the word mapDisplay the reaction diagram Show all sequences 2.7.8.43? x * 60000, about, sequence calculation -, 739495
Display the word mapDisplay the reaction diagram Show all sequences 2.7.8.43More 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
Display the word mapDisplay the reaction diagram Show all sequences 2.7.8.43More enzyme structure analysis, overview -, 739786
Display the word mapDisplay the reaction diagram Show all sequences 2.7.8.43More 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
Display the word mapDisplay the reaction diagram Show all sequences 2.7.8.43More 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
Display the word mapDisplay the reaction diagram Show all sequences 2.7.8.43oligomer 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
Results 1 - 7 of 7