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| | <StructureSection load='5hbu' size='340' side='right'caption='[[5hbu]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='5hbu' size='340' side='right'caption='[[5hbu]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5hbu]] is a 13 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HBU OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5HBU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5hbu]] is a 13 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] 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=5HBU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HBU FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5haw|5haw]]</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]] 2.6Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">slmA, ttk, yicB, b3641, JW5641 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=5hbu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hbu OCA], [https://pdbe.org/5hbu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hbu RCSB], [https://www.ebi.ac.uk/pdbsum/5hbu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hbu ProSAT]</span></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=5hbu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hbu OCA], [http://pdbe.org/5hbu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hbu RCSB], [http://www.ebi.ac.uk/pdbsum/5hbu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hbu ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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> | + | [https://www.uniprot.org/uniprot/FTSZ_ECOLI FTSZ_ECOLI] Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity. Polymerization and bundle formation is enhanced by CbeA.[HAMAP-Rule:MF_00909] |
| | <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: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Schumacher, M A]] | + | [[Category: Synthetic construct]] |
| - | [[Category: Zeng, W]] | + | [[Category: Schumacher MA]] |
| - | [[Category: Cell cycle-dna complex]] | + | [[Category: Zeng W]] |
| - | [[Category: Cytokinesis]]
| + | |
| - | [[Category: Ftsz]]
| + | |
| - | [[Category: Nucleoid occlusion]]
| + | |
| - | [[Category: Slma]]
| + | |
| Structural highlights
Function
FTSZ_ECOLI Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity. Polymerization and bundle formation is enhanced by CbeA.[HAMAP-Rule:MF_00909]
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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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