EC Number |
Subunits |
Reference |
---|
2.4.1.12 | ? |
x * 100000, SDS-PAGE |
758221 |
2.4.1.12 | ? |
x * 110500, calculated from amino acid sequence |
758221 |
2.4.1.12 | ? |
x * 130000, His6-tagged enzyme, SDS-PAGE |
757973 |
2.4.1.12 | ? |
x * 164000, SDS-PAGE |
755703 |
2.4.1.12 | ? |
x * 93000 + x * 83000, subunits AcsB and AcsA, SDS-PAGE |
-, 758133 |
2.4.1.12 | dimer |
alphabeta, 1 * 83000 + 1 * 93000, SDS-PAGE |
637175 |
2.4.1.12 | dimer |
BcsA and BcsB form a 1:1 stoichiometric complex spanning approximately 150 A perpendicular and 55 A parallel to the membrane. The complex is divided into a cuboid-shaped membrane-spanning region sandwiched between large cytoplasmic and periplasmic domains. BcsA contains four N-terminal and four C-terminal transmembrane-helices separated by a large intracellular loop (4/5-loop) that forms a GT-domain (aa 128 to 368). transmembrane domains 3-8 form a narrow channel for the translocating polysaccharide and BcsA's intracellular C-terminus (aa 575 to 759) contains a 6-stranded beta-barrel and a highly curved alpha-helical region that attaches the beta-barrel to the GT-domain. BcsB is a dome-shaped, beta-strand rich, periplasmic protein. Its N-terminal region forms the tip of the dome, whereas the C-terminal transmembrane-anchor interacts with BcsA. Two amphipathic helices further stabilize its interaction with BcsA and the periplasmic water-membrane interface. Domain structures. Modeling, overview |
736877 |
2.4.1.12 | dimer |
recombinant catalytic domains of rice CesA8 cellulose synthase form dimers reversibly as the fundamental scaffold units of architecture in the synthase complex. The monomer is a two-domain, elongated structure, with the smaller domain coupling two monomers into a dimer. The catalytic core of the monomer is accommodated only near its center, with the plant-specific sequences occupying the small domain and an extension distal to the catalytic domain, structure comparison and modeling, overview. Proposed role for dimers in particle rosette assembly |
736991 |
2.4.1.12 | homodimer |
isozyme CESA4 |
703730 |
2.4.1.12 | monomer |
isozyme CESA7 |
703730 |