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| - | ==Regulatory CZB domain of YdeH== | + | |
| - | <StructureSection load='3t9o' size='340' side='right' caption='[[3t9o]], [[Resolution|resolution]] 2.20Å' scene=''> | + | ==Regulatory CZB domain of DgcZ== |
| | + | <StructureSection load='3t9o' size='340' side='right'caption='[[3t9o]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3t9o]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T9O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3T9O FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3t9o]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T9O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T9O FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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]] 2.2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b1535, JW1528, ydeG, ydeH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Diguanylate_kinase Diguanylate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.65 2.7.7.65] </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=3t9o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t9o OCA], [https://pdbe.org/3t9o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t9o RCSB], [https://www.ebi.ac.uk/pdbsum/3t9o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t9o 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=3t9o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t9o OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3t9o RCSB], [http://www.ebi.ac.uk/pdbsum/3t9o PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/DGCZ_ECOLI DGCZ_ECOLI] Catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules (PubMed:18713317, PubMed:19460094, PubMed:20582742). May act as a zinc sensor that controls, via c-di-GMP, post-translational events (PubMed:23769666). Overexpression leads to a strong repression of swimming; swimming returnes to normal when residues 206-207 are both mutated to Ala. Overexpression also leads to a reduction in flagellar abundance and a 20-fold increase in c-di-GMP levels in vivo. Required for aminoglycoside-mediated induction of biofilm formation, it also plays a lesser role in biofilm production in response to other classes of translation inhibitors. The c-di-GMP produced by this enzyme up-regulates poly-GlcNAc production as well as the biofilm synthesis protein PgaD, although c-di-GMP is probably not the main inducing principle. C-di-GMP is a second messenger which controls cell surface-associated traits in bacteria (PubMed:19460094).<ref>PMID:19460094</ref> <ref>PMID:20582742</ref> <ref>PMID:23769666</ref> <ref>PMID:18713317</ref> |
| | + | |
| | + | ==See Also== |
| | + | *[[Diguanylate cyclase|Diguanylate cyclase]] |
| | + | == References == |
| | + | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Diguanylate kinase]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: Escherichia coli]] | + | [[Category: Large Structures]] |
| - | [[Category: Schirmer, T]] | + | [[Category: Schirmer T]] |
| - | [[Category: Zaehringer, F]] | + | [[Category: Zaehringer F]] |
| - | [[Category: Czb domain]]
| + | |
| - | [[Category: Diguanylate cyclase]]
| + | |
| - | [[Category: Metal binding protein]]
| + | |
| - | [[Category: Putative zinc sensor]]
| + | |
| Structural highlights
Function
DGCZ_ECOLI Catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules (PubMed:18713317, PubMed:19460094, PubMed:20582742). May act as a zinc sensor that controls, via c-di-GMP, post-translational events (PubMed:23769666). Overexpression leads to a strong repression of swimming; swimming returnes to normal when residues 206-207 are both mutated to Ala. Overexpression also leads to a reduction in flagellar abundance and a 20-fold increase in c-di-GMP levels in vivo. Required for aminoglycoside-mediated induction of biofilm formation, it also plays a lesser role in biofilm production in response to other classes of translation inhibitors. The c-di-GMP produced by this enzyme up-regulates poly-GlcNAc production as well as the biofilm synthesis protein PgaD, although c-di-GMP is probably not the main inducing principle. C-di-GMP is a second messenger which controls cell surface-associated traits in bacteria (PubMed:19460094).[1] [2] [3] [4]
See Also
References
- ↑ Boehm A, Steiner S, Zaehringer F, Casanova A, Hamburger F, Ritz D, Keck W, Ackermann M, Schirmer T, Jenal U. Second messenger signalling governs Escherichia coli biofilm induction upon ribosomal stress. Mol Microbiol. 2009 Jun;72(6):1500-16. doi: 10.1111/j.1365-2958.2009.06739.x., Epub 2009 May 15. PMID:19460094 doi:10.1111/j.1365-2958.2009.06739.x
- ↑ Zahringer F, Massa C, Schirmer T. Efficient enzymatic production of the bacterial second messenger c-di-GMP by the diguanylate cyclase YdeH from E. coli. Appl Biochem Biotechnol. 2011 Jan;163(1):71-9. doi: 10.1007/s12010-010-9017-x., Epub 2010 Jun 29. PMID:20582742 doi:http://dx.doi.org/10.1007/s12010-010-9017-x
- ↑ Zahringer F, Lacanna E, Jenal U, Schirmer T, Boehm A. Structure and Signaling Mechanism of a Zinc-Sensory Diguanylate Cyclase. Structure. 2013 Jun 11. pii: S0969-2126(13)00156-1. doi:, 10.1016/j.str.2013.04.026. PMID:23769666 doi:10.1016/j.str.2013.04.026
- ↑ Jonas K, Edwards AN, Simm R, Romeo T, Romling U, Melefors O. The RNA binding protein CsrA controls cyclic di-GMP metabolism by directly regulating the expression of GGDEF proteins. Mol Microbiol. 2008 Oct;70(1):236-57. doi: 10.1111/j.1365-2958.2008.06411.x. Epub, 2008 Aug 18. PMID:18713317 doi:http://dx.doi.org/10.1111/j.1365-2958.2008.06411.x
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