EC Number |
Subunits |
Reference |
---|
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 | More |
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 | More |
enzyme structure analysis, overview |
-, 739786 |
2.7.8.43 | More |
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 | More |
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 |