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Results 1 - 8 of 8
EC Number
Subunits
Commentary
Reference
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x * 36700, recombinant His-tagged wild-type, SDS-PAGE
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x * 60000, about, sequence calculation
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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
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enzyme structure analysis, overview
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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
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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; 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
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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
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
Results 1 - 8 of 8