|
|
| (One intermediate revision not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==Crystal structure of PilZ domain of CeSA from cellulose synthesizing bacterium== | | ==Crystal structure of PilZ domain of CeSA from cellulose synthesizing bacterium== |
| - | <StructureSection load='4i86' size='340' side='right' caption='[[4i86]], [[Resolution|resolution]] 2.10Å' scene=''> | + | <StructureSection load='4i86' size='340' side='right'caption='[[4i86]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4i86]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"acetobacter_bordeaux"_(sic)_janke_1957 "acetobacter bordeaux" (sic) janke 1957]. 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 [http://oca.weizmann.ac.il/oca-docs/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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">acsAB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=28448 "Acetobacter bordeaux" (sic) Janke 1957])</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellulose_synthase_(UDP-forming) Cellulose synthase (UDP-forming)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.12 2.4.1.12] </span></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> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4i86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i86 OCA], [http://pdbe.org/4i86 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4i86 RCSB], [http://www.ebi.ac.uk/pdbsum/4i86 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4i86 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ACSA1_GLUXY ACSA1_GLUXY]] 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). | + | [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.
| + | |
| - | | + | |
| - | 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>
| + | |
| - | | + | |
| - | 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/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Fujiwara, T]] | + | [[Category: Komagataeibacter xylinus]] |
| - | [[Category: Komoda, K]] | + | [[Category: Large Structures]] |
| - | [[Category: Sakurai, N]] | + | [[Category: Fujiwara T]] |
| - | [[Category: Tanaka, I]] | + | [[Category: Komoda K]] |
| - | [[Category: Yao, M]] | + | [[Category: Sakurai N]] |
| - | [[Category: Beta-barrel fold]] | + | [[Category: Tanaka I]] |
| - | [[Category: C-di-gmp binding]] | + | [[Category: Yao M]] |
| - | [[Category: Transferase]]
| + | |
