4i86
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4i86]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Komagataeibacter_xylinus Komagataeibacter xylinus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4I86 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4I86 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4i86]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Komagataeibacter_xylinus Komagataeibacter xylinus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4I86 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4I86 FirstGlance]. <br> | ||
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4i86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i86 OCA], [https://pdbe.org/4i86 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4i86 RCSB], [https://www.ebi.ac.uk/pdbsum/4i86 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4i86 ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.098Å</td></tr> |
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4i86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i86 OCA], [https://pdbe.org/4i86 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4i86 RCSB], [https://www.ebi.ac.uk/pdbsum/4i86 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4i86 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/ACSA1_KOMXY ACSA1_KOMXY] Bifunctional protein comprised of a catalytic subunit and a regulatory subunit. The catalytic subunit of cellulose synthase polymerizes uridine 5'-diphosphate glucose to cellulose in a processive way. The thick cellulosic mats generated by this enzyme probably provide a specialized protective environment to the bacterium. The regulatory subunit binds bis-(3'-5') cyclic diguanylic acid (c-di-GMP).<ref>PMID:2138620</ref> | [https://www.uniprot.org/uniprot/ACSA1_KOMXY ACSA1_KOMXY] Bifunctional protein comprised of a catalytic subunit and a regulatory subunit. The catalytic subunit of cellulose synthase polymerizes uridine 5'-diphosphate glucose to cellulose in a processive way. The thick cellulosic mats generated by this enzyme probably provide a specialized protective environment to the bacterium. The regulatory subunit binds bis-(3'-5') cyclic diguanylic acid (c-di-GMP).<ref>PMID:2138620</ref> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | 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 2.1A 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. | ||
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| - | The c-di-GMP recognition mechanism of the PilZ domain of bacterial cellulose synthase subunit A.,Fujiwara T, Komoda K, Sakurai N, Tajima K, Tanaka I, Yao M Biochem Biophys Res Commun. 2013 Feb 22;431(4):802-7. doi:, 10.1016/j.bbrc.2012.12.103. Epub 2013 Jan 4. PMID:23291177<ref>PMID:23291177</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4i86" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Crystal structure of PilZ domain of CeSA from cellulose synthesizing bacterium
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