5hbu
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of the E. coli nucleoid occlusion protein SlmA bound to DNA and the C-terminal tail of the cytoskeletal cell division protein FtsZ== | |
| + | <StructureSection load='5hbu' size='340' side='right' caption='[[5hbu]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5hbu]] is a 13 chain structure. 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://oca.weizmann.ac.il/oca-docs/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> | ||
| + | <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=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]</span></td></tr> | ||
| + | </table> | ||
| + | == 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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:27091999</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: Schumacher, M | + | <div class="pdbe-citations 5hbu" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Schumacher, M A]] | ||
[[Category: Zeng, W]] | [[Category: Zeng, W]] | ||
| + | [[Category: Cell cycle-dna complex]] | ||
| + | [[Category: Cytokinesis]] | ||
| + | [[Category: Ftsz]] | ||
| + | [[Category: Nucleoid occlusion]] | ||
| + | [[Category: Slma]] | ||
Revision as of 16:11, 10 May 2016
Structure of the E. coli nucleoid occlusion protein SlmA bound to DNA and the C-terminal tail of the cytoskeletal cell division protein FtsZ
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