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| | ==Solution structure of the Carbon Storage Regulator protein CsrA== | | ==Solution structure of the Carbon Storage Regulator protein CsrA== |
| - | <StructureSection load='1y00' size='340' side='right'caption='[[1y00]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='1y00' size='340' side='right'caption='[[1y00]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1y00]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y00 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y00 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1y00]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y00 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y00 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">csrA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1y00 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y00 OCA], [https://pdbe.org/1y00 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y00 RCSB], [https://www.ebi.ac.uk/pdbsum/1y00 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y00 ProSAT], [https://www.topsan.org/Proteins/BSGI/1y00 TOPSAN]</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=1y00 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y00 OCA], [https://pdbe.org/1y00 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y00 RCSB], [https://www.ebi.ac.uk/pdbsum/1y00 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y00 ProSAT], [https://www.topsan.org/Proteins/BSGI/1y00 TOPSAN]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/CSRA_ECOLI CSRA_ECOLI]] Binds to mRNA to regulate post-transcriptional activity. Affects glycogen biosynthesis, gluconeogenesis, cell size and surface properties. Regulates glycogen synthesis under both aerobic and anaerobic conditions. Seems to accelerate the degradation of glg gene transcripts, potentially through selective RNA binding. Acts to inhibit interaction between the LetD protein and the A subunit of DNA gyrase. Also required for motility and flagellum biosynthesis through the post-transcriptional activation of flhDC expression. This involves binding to and stabilization of the flhDC message by CsrA. Binds to and reduces levels of probable diguanylate cyclases ycdT and ydeH.<ref>PMID:11298291</ref> <ref>PMID:18713317</ref> <ref>PMID:19460094</ref>
| + | [https://www.uniprot.org/uniprot/CSRA_ECOLI CSRA_ECOLI] Binds to mRNA to regulate post-transcriptional activity. Affects glycogen biosynthesis, gluconeogenesis, cell size and surface properties. Regulates glycogen synthesis under both aerobic and anaerobic conditions. Seems to accelerate the degradation of glg gene transcripts, potentially through selective RNA binding. Acts to inhibit interaction between the LetD protein and the A subunit of DNA gyrase. Also required for motility and flagellum biosynthesis through the post-transcriptional activation of flhDC expression. This involves binding to and stabilization of the flhDC message by CsrA. Binds to and reduces levels of probable diguanylate cyclases ycdT and ydeH.<ref>PMID:11298291</ref> <ref>PMID:18713317</ref> <ref>PMID:19460094</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Structural genomic]]
| + | [[Category: Gehring K]] |
| - | [[Category: Gehring, K]] | + | [[Category: Gutierrez P]] |
| - | [[Category: Gutierrez, P]] | + | [[Category: Li Y]] |
| - | [[Category: Li, Y]] | + | [[Category: Liu Q]] |
| - | [[Category: Liu, Q]] | + | [[Category: Osborne MJ]] |
| - | [[Category: Osborne, M J]] | + | |
| - | [[Category: Bsgi]]
| + | |
| - | [[Category: Carbon storage regulation]]
| + | |
| - | [[Category: Rna binding protein]]
| + | |
| Structural highlights
Function
CSRA_ECOLI Binds to mRNA to regulate post-transcriptional activity. Affects glycogen biosynthesis, gluconeogenesis, cell size and surface properties. Regulates glycogen synthesis under both aerobic and anaerobic conditions. Seems to accelerate the degradation of glg gene transcripts, potentially through selective RNA binding. Acts to inhibit interaction between the LetD protein and the A subunit of DNA gyrase. Also required for motility and flagellum biosynthesis through the post-transcriptional activation of flhDC expression. This involves binding to and stabilization of the flhDC message by CsrA. Binds to and reduces levels of probable diguanylate cyclases ycdT and ydeH.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The carbon storage regulator A (CsrA) is a protein responsible for the repression of a variety of stationary-phase genes in bacteria. In this work, we describe the nuclear magnetic resonance (NMR)-based structure of the CsrA dimer and its RNA-binding properties. CsrA is a dimer of two identical subunits, each composed of five strands, a small alpha-helix and a flexible C terminus. NMR titration experiments suggest that the beta1-beta2 and beta3-beta4 loops and the C-terminal helix are important elements in RNA binding. Even though the beta3-beta4 loop contains a highly conserved RNA-binding motif, GxxG, typical of KH domains, our structure excludes CsrA from being a member of this protein family, as previously suggested. A mechanism for the recognition of mRNAs downregulated by CsrA is proposed.
Solution structure of the carbon storage regulator protein CsrA from Escherichia coli.,Gutierrez P, Li Y, Osborne MJ, Pomerantseva E, Liu Q, Gehring K J Bacteriol. 2005 May;187(10):3496-501. PMID:15866937[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wei BL, Brun-Zinkernagel AM, Simecka JW, Pruss BM, Babitzke P, Romeo T. Positive regulation of motility and flhDC expression by the RNA-binding protein CsrA of Escherichia coli. Mol Microbiol. 2001 Apr;40(1):245-56. PMID:11298291
- ↑ 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
- ↑ 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
- ↑ Gutierrez P, Li Y, Osborne MJ, Pomerantseva E, Liu Q, Gehring K. Solution structure of the carbon storage regulator protein CsrA from Escherichia coli. J Bacteriol. 2005 May;187(10):3496-501. PMID:15866937 doi:187/10/3496
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