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| | <StructureSection load='5k58' size='340' side='right'caption='[[5k58]], [[Resolution|resolution]] 2.77Å' scene=''> | | <StructureSection load='5k58' size='340' side='right'caption='[[5k58]], [[Resolution|resolution]] 2.77Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5k58]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Eco24 Eco24]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K58 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5K58 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5k58]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O139:H28_str._E24377A Escherichia coli O139:H28 str. E24377A] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K58 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5K58 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">slmA, EcE24377A_4142 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=331111 ECO24])</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]] 2.772Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5k58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k58 OCA], [http://pdbe.org/5k58 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k58 RCSB], [http://www.ebi.ac.uk/pdbsum/5k58 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5k58 ProSAT]</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=5k58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k58 OCA], [https://pdbe.org/5k58 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5k58 RCSB], [https://www.ebi.ac.uk/pdbsum/5k58 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5k58 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SLMA_ECO24 SLMA_ECO24]] Required for nucleoid occlusion (NO) phenomenon, which prevents Z-ring formation and cell division over the nucleoid. Acts as a DNA-associated cell division inhibitor that binds simultaneously chromosomal DNA and FtsZ, and disrupts the assembly of FtsZ polymers. SlmA-DNA-binding sequences (SBS) are dispersed on non-Ter regions of the chromosome, preventing FtsZ polymerization at these regions. | + | [https://www.uniprot.org/uniprot/SLMA_ECOLI SLMA_ECOLI] Required for nucleoid occlusion (NO) phenomenon, which prevents Z-ring formation and cell division over the nucleoid. Acts as a DNA-associated cell division inhibitor that binds simultaneously chromosomal DNA and FtsZ, and disrupts the assembly of FtsZ polymers. SlmA-DNA-binding sequences (SBS) are dispersed on non-Ter regions of the chromosome, preventing FtsZ polymerization at these regions.[HAMAP-Rule:MF_01839]<ref>PMID:15916962</ref> <ref>PMID:21113127</ref> <ref>PMID:21321206</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Eco24]] | + | [[Category: Escherichia coli O139:H28 str. E24377A]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Schumacher, M]] | + | [[Category: Synthetic construct]] |
| - | [[Category: Dna]] | + | [[Category: Schumacher M]] |
| - | [[Category: Dna binding protein-dna complex]]
| + | |
| - | [[Category: Ftsz]]
| + | |
| - | [[Category: Nucleoid occlusion]]
| + | |
| - | [[Category: Slma]]
| + | |
| Structural highlights
Function
SLMA_ECOLI Required for nucleoid occlusion (NO) phenomenon, which prevents Z-ring formation and cell division over the nucleoid. Acts as a DNA-associated cell division inhibitor that binds simultaneously chromosomal DNA and FtsZ, and disrupts the assembly of FtsZ polymers. SlmA-DNA-binding sequences (SBS) are dispersed on non-Ter regions of the chromosome, preventing FtsZ polymerization at these regions.[HAMAP-Rule:MF_01839][1] [2] [3]
Publication Abstract from PubMed
Cell division in most prokaryotes is mediated by FtsZ, which polymerizes to create the cytokinetic Z ring. Multiple FtsZ-binding proteins regulate FtsZ polymerization to ensure the proper spatiotemporal formation of the Z ring at the division site. The DNA-binding protein SlmA binds to FtsZ and prevents Z-ring formation through the nucleoid in a process called "nucleoid occlusion" (NO). As do most FtsZ-accessory proteins, SlmA interacts with the conserved C-terminal domain (CTD) that is connected to the FtsZ core by a long, flexible linker. However, SlmA is distinct from other regulatory factors in that it must be DNA-bound to interact with the FtsZ CTD. Few structures of FtsZ regulator-CTD complexes are available, but all reveal the CTD bound as a helix. To deduce the molecular basis for the unique SlmA-DNA-FtsZ CTD regulatory interaction and provide insight into FtsZ-regulator protein complex formation, we determined structures of Escherichia coli, Vibrio cholera, and Klebsiella pneumonia SlmA-DNA-FtsZ CTD ternary complexes. Strikingly, the FtsZ CTD does not interact with SlmA as a helix but binds as an extended conformation in a narrow, surface-exposed pocket formed only in the DNA-bound state of SlmA and located at the junction between the DNA-binding and C-terminal dimer domains. Binding studies are consistent with the structure and underscore key interactions in complex formation. Combined, these data reveal the molecular basis for the SlmA-DNA-FtsZ interaction with implications for SlmA's NO function and underscore the ability of the FtsZ CTD to adopt a wide range of conformations, explaining its ability to bind diverse regulatory proteins.
Structures of the nucleoid occlusion protein SlmA bound to DNA and the C-terminal domain of the cytoskeletal protein FtsZ.,Schumacher MA, Zeng W Proc Natl Acad Sci U S A. 2016 May 3;113(18):4988-93. doi:, 10.1073/pnas.1602327113. Epub 2016 Apr 18. PMID:27091999[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bernhardt TG, de Boer PA. SlmA, a nucleoid-associated, FtsZ binding protein required for blocking septal ring assembly over Chromosomes in E. coli. Mol Cell. 2005 May 27;18(5):555-64. PMID:15916962 doi:http://dx.doi.org/S1097-2765(05)01275-X
- ↑ Tonthat NK, Arold ST, Pickering BF, Van Dyke MW, Liang S, Lu Y, Beuria TK, Margolin W, Schumacher MA. Molecular mechanism by which the nucleoid occlusion factor, SlmA, keeps cytokinesis in check. EMBO J. 2011 Jan 5;30(1):154-64. Epub 2010 Nov 26. PMID:21113127 doi:10.1038/emboj.2010.288
- ↑ Cho H, McManus HR, Dove SL, Bernhardt TG. Nucleoid occlusion factor SlmA is a DNA-activated FtsZ polymerization antagonist. Proc Natl Acad Sci U S A. 2011 Mar 1;108(9):3773-8. doi: 10.1073/pnas.1018674108., Epub 2011 Feb 14. PMID:21321206 doi:http://dx.doi.org/10.1073/pnas.1018674108
- ↑ Schumacher MA, Zeng W. Structures of the nucleoid occlusion protein SlmA bound to DNA and the C-terminal domain of the cytoskeletal protein FtsZ. Proc Natl Acad Sci U S A. 2016 May 3;113(18):4988-93. doi:, 10.1073/pnas.1602327113. Epub 2016 Apr 18. PMID:27091999 doi:http://dx.doi.org/10.1073/pnas.1602327113
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