This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

4i86

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 08:47, 9 November 2022

Crystal structure of PilZ domain of CeSA from cellulose synthesizing bacterium

Structural highlights

4i86 is a 2 chain structure with sequence from Komagataeibacter xylinus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).^[1]

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Lin FC, Brown RM Jr, Drake RR Jr, Haley BE. Identification of the uridine 5'-diphosphoglucose (UDP-Glc) binding subunit of cellulose synthase in Acetobacter xylinum using the photoaffinity probe 5-azido-UDP-Glc. J Biol Chem. 1990 Mar 25;265(9):4782-4. PMID:2138620
↑ 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. 2013 Feb 22;431(4):802-7. doi:, 10.1016/j.bbrc.2012.12.103. Epub 2013 Jan 4. PMID:23291177 doi:http://dx.doi.org/10.1016/j.bbrc.2012.12.103

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4i86"

@@ Line 1: / Line 1: @@
 ==Crystal structure of PilZ domain of CeSA from cellulose synthesizing bacterium==
-<StructureSection load='4i86' size='340' side='right' caption='[[4i86]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
+<StructureSection load='4i86' size='340' side='right'caption='[[4i86]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == 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='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='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://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>
 == 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 ==
@@ Line 23: / Line 21: @@
 __TOC__
 </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]]

4i86

From Proteopedia

Revision as of 08:47, 9 November 2022

Crystal structure of PilZ domain of CeSA from cellulose synthesizing bacterium

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox