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
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
existence of binding sites for three distinct CESA subunits in primary wall cellulose synthase complexes, with two positions being invariably occupied by CESA1 and CESA3, whereas at least three isoforms compete for the third position
existence of binding sites for three distinct CESA subunits in primary wall cellulose synthase complexes, with two positions being invariably occupied by CESA1 and CESA3, whereas at least three isoforms compete for the third position
existence of binding sites for three distinct CESA subunits in primary wall cellulose synthase complexes, with two positions being invariably occupied by CESA1 and CESA3, whereas at least three isoforms compete for the third position
cellulose synthase A is a catalytic component of the cellulose synthase complex. Mass spectrometric analysis of purified cellulose synthase components, His- and STREP-tagged CESA4, CESA7, and CESA8 from irx1-1, irx3-1, and irx5-2 mutant plants, overview
secondary CESA proteins are organized in the rosette structure. Although all CESA proteins can interact with each other, only CESA4 is able to form homodimers
secondary CESA proteins are organized in the rosette structure. Although all CESA proteins can interact with each other, only CESA4 is able to form homodimers
secondary CESA proteins are organized in the rosette structure. Although all CESA proteins can interact with each other, only CESA4 is able to form homodimers
CesA isozymes all contains the D,D,D,QXXRW signature, their N-terminal ends exhibited oomycete-specific domains, i.e. Pleckstrin homology domains, or conserved domains of an unknown function together with additional putative transmembrane domains
CesA isozymes all contains the D,D,D,QXXRW signature, their N-terminal ends exhibited oomycete-specific domains, i.e. Pleckstrin homology domains, or conserved domains of an unknown function together with additional putative transmembrane domains
CesA isozymes all contains the D,D,D,QXXRW signature, their N-terminal ends exhibited oomycete-specific domains, i.e. Pleckstrin homology domains, or conserved domains of an unknown function together with additional putative transmembrane domains
SpCesa1 contains an N-terminal cysteine-rich zinc binding domain, seven putative transmembrane helices, four U-motifs containing the conserved siganture DDDQXXRW, 1 conserved and two hypervariable regions