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| | <StructureSection load='5haw' size='340' side='right'caption='[[5haw]], [[Resolution|resolution]] 1.89Å' scene=''> | | <StructureSection load='5haw' size='340' side='right'caption='[[5haw]], [[Resolution|resolution]] 1.89Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5haw]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Vibch Vibch]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HAW OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5HAW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5haw]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae_O1_biovar_El_Tor_str._N16961 Vibrio cholerae O1 biovar El Tor str. N16961] 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=5HAW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HAW FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5hbu|5hbu]]</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=5haw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5haw OCA], [https://pdbe.org/5haw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5haw RCSB], [https://www.ebi.ac.uk/pdbsum/5haw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5haw ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">slmA, VC_0214 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243277 VIBCH])</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=5haw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5haw OCA], [http://pdbe.org/5haw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5haw RCSB], [http://www.ebi.ac.uk/pdbsum/5haw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5haw ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SLMA_VIBCH SLMA_VIBCH]] 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 (By similarity). | + | [https://www.uniprot.org/uniprot/SLMA_VIBCH SLMA_VIBCH] 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 (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Vibch]] | + | [[Category: Synthetic construct]] |
| - | [[Category: Schumacher, M A]] | + | [[Category: Vibrio cholerae O1 biovar El Tor str. N16961]] |
| - | [[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
SLMA_VIBCH 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 (By similarity).
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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