4i86
From Proteopedia
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| - | + | ==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=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4i86]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Gluconacetobacter_xylinus Gluconacetobacter 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4I86 FirstGlance]. <br> | |
| - | ==Function== | + | </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 Gluconacetobacter xylinus])</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'>[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://www.rcsb.org/pdb/explore.do?structureId=4i86 RCSB], [http://www.ebi.ac.uk/pdbsum/4i86 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == 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). | [[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). | ||
| + | <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> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Gluconacetobacter xylinus]] | [[Category: Gluconacetobacter xylinus]] | ||
| - | [[Category: Fujiwara, T | + | [[Category: Fujiwara, T]] |
| - | [[Category: Komoda, K | + | [[Category: Komoda, K]] |
| - | [[Category: Sakurai, N | + | [[Category: Sakurai, N]] |
| - | [[Category: Tanaka, I | + | [[Category: Tanaka, I]] |
| - | [[Category: Yao, M | + | [[Category: Yao, M]] |
[[Category: Beta-barrel fold]] | [[Category: Beta-barrel fold]] | ||
[[Category: C-di-gmp binding]] | [[Category: C-di-gmp binding]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 01:26, 25 December 2014
Crystal structure of PilZ domain of CeSA from cellulose synthesizing bacterium
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