4I86

Crystal structure of PilZ domain of CeSA from cellulose synthesizing bacterium

Summary for 4I86

• Entry DOI: 10.2210/pdb4i86/pdb
• Descriptor: Cellulose synthase 1 (2 entities in total)
• Functional Keywords: beta-barrel fold, c-di-gmp binding, transferase
• Biological source: Gluconacetobacter xylinus
• Cellular location: Cell inner membrane; Multi-pass membrane protein (Potential): P0CW87
• Total number of polymer chains: 2
• Total formula weight: 24590.24

Authors

Fujiwara, T.,Komoda, K.,Sakurai, N.,Tanaka, I.,Yao, M. (deposition date: 2012-12-03, release date: 2013-04-03, Last modification date: 2024-03-20)

Primary citation

Fujiwara, T.,Komoda, K.,Sakurai, N.,Tajima, K.,Tanaka, I.,Yao, M.
The c-di-GMP recognition mechanism of the PilZ domain of bacterial cellulose synthase subunit A
Biochem.Biophys.Res.Commun., 431:802-807, 2013

PubMed Abstract: In some Proteobacteria and Firmicutes such as Pseudomonas aeruginosa, Vibrio cholerae, Xanthomonas campestris, and Clostridium difficile, cyclic dimeric guanosine monophosphate (c-di-GMP) is known to regulate cellular processes, including motility, biofilm formation, and virulence, as a second messenger. Cellulose production in Acetobacter xylinum, a model organism of cellulose biosynthesis, also depends on by cellular c-di-GMP level. In cellulose-synthesizing bacteria, a terminal complex localized in the cell membrane synthesizes cellulose and regulates the production of cellulose sensed by c-di-GMP. Although previous studies indicated that the PilZ domain conserved in cellulose synthase subunit A (CeSA) was part of a receptor for c-di-GMP, the recognition mechanism by PilZ domain of CeSA remains unclear. In the present study, we studied the interaction between c-di-GMP and the PilZ domain of CeSA from a structural viewpoint. First, we solved the crystal structure of the PilZ domain of CeSA from A. xylinum (AxCeSA-PilZ) at 2.1Å resolution. Then, comparison of the sequence and structure of AxCeSA-PilZ to those of known structures of PilZ, such as VCA0042, PP4397, and PA4608, indicated the involvement of Lys573 and Arg643 of AxCeSA-PilZ in the recognition of c-di-GMP besides the RxxxR motif. Finally, the binding characteristics of c-di-GMP to AxCeSA-PilZ and mutants were determined with isothermal titration calorimetry, indicating that the residues corresponding to Lys573 and Arg643 in AxCeSA-PilZ generally contribute to the binding of c-di-GMP to PilZ.

PubMed: 23291177
DOI: 10.1016/j.bbrc.2012.12.103

Experimental method

X-RAY DIFFRACTION (2.098 Å)