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| | ==Bacillus subtilis SepF, C-terminal domain== | | ==Bacillus subtilis SepF, C-terminal domain== |
| - | <StructureSection load='3zih' size='340' side='right' caption='[[3zih]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='3zih' size='340' side='right'caption='[[3zih]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3zih]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZIH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZIH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3zih]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZIH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZIH FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3zie|3zie]], [[3zig|3zig]], [[3zii|3zii]]</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]] 2Å</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=3zih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zih OCA], [http://pdbe.org/3zih PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3zih RCSB], [http://www.ebi.ac.uk/pdbsum/3zih PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3zih 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=3zih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zih OCA], [https://pdbe.org/3zih PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zih RCSB], [https://www.ebi.ac.uk/pdbsum/3zih PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zih ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SEPF_BACSU SEPF_BACSU]] Cell division protein that is part of the divisome complex and is recruited early to the Z-ring. Probably stimulates Z-ring formation, perhaps through the cross-linking of FtsZ protofilaments. Its function overlaps with FtsA.<ref>PMID:16420366</ref> <ref>PMID:16796675</ref> | + | [https://www.uniprot.org/uniprot/SEPF_BACSU SEPF_BACSU] Cell division protein that is part of the divisome complex and is recruited early to the Z-ring. Probably stimulates Z-ring formation, perhaps through the cross-linking of FtsZ protofilaments. Its function overlaps with FtsA.<ref>PMID:16420366</ref> <ref>PMID:16796675</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 3zih" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 3zih" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Cell division protein 3D structures|Cell division protein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus globigii migula 1900]] | + | [[Category: Bacillus subtilis]] |
| - | [[Category: Celik, I]] | + | [[Category: Large Structures]] |
| - | [[Category: Duman, R E]] | + | [[Category: Celik I]] |
| - | [[Category: Hamoen, L W]] | + | [[Category: Duman RE]] |
| - | [[Category: Ishikawa, S]] | + | [[Category: Hamoen LW]] |
| - | [[Category: Lowe, J]] | + | [[Category: Ishikawa S]] |
| - | [[Category: Ogasawara, N]] | + | [[Category: Lowe J]] |
| - | [[Category: Cell cycle]]
| + | [[Category: Ogasawara N]] |
| Structural highlights
Function
SEPF_BACSU Cell division protein that is part of the divisome complex and is recruited early to the Z-ring. Probably stimulates Z-ring formation, perhaps through the cross-linking of FtsZ protofilaments. Its function overlaps with FtsA.[1] [2]
Publication Abstract from PubMed
A key step in bacterial cell division is the polymerization of the tubulin homolog FtsZ at midcell. FtsZ polymers are anchored to the cell membrane by FtsA and are required for the assembly of all other cell division proteins. In Gram-positive and cyanobacteria, FtsZ filaments are aligned by the protein SepF, which in vitro polymerizes into large rings that bundle FtsZ filaments. Here we describe the crystal structure of the only globular domain of SepF, located within the C-terminal region. Two-hybrid data revealed that this domain comprises the FtsZ binding site, and EM analyses showed that it is sufficient for ring formation, which is explained by the filaments in the crystals of SepF. Site-directed mutagenesis, gel filtration, and analytical ultracentrifugation indicated that dimers form the basic units of SepF filaments. High-resolution structured illumination microscopy suggested that SepF is membrane associated, and it turned out that purified SepF not only binds to lipid membranes, but also recruits FtsZ. Further genetic and biochemical analyses showed that an amphipathic helix at the N terminus functions as the membrane-binding domain, making SepF a unique membrane anchor for the FtsZ ring. This clarifies why Bacillus subtilis grows without FtsA or the putative membrane anchor EzrA and why bacteria lacking FtsA contain SepF homologs. Both FtsA and SepF use an amphipathic helix for membrane binding. These helices prefer positively curved membranes due to relaxed lipid density; therefore this type of membrane anchor may assist in keeping the Z ring positioned at the strongly curved leading edge of the developing septum.
Structural and genetic analyses reveal the protein SepF as a new membrane anchor for the Z ring.,Duman R, Ishikawa S, Celik I, Strahl H, Ogasawara N, Troc P, Lowe J, Hamoen LW Proc Natl Acad Sci U S A. 2013 Nov 11. PMID:24218584[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hamoen LW, Meile JC, de Jong W, Noirot P, Errington J. SepF, a novel FtsZ-interacting protein required for a late step in cell division. Mol Microbiol. 2006 Feb;59(3):989-99. PMID:16420366 doi:http://dx.doi.org/10.1111/j.1365-2958.2005.04987.x
- ↑ Ishikawa S, Kawai Y, Hiramatsu K, Kuwano M, Ogasawara N. A new FtsZ-interacting protein, YlmF, complements the activity of FtsA during progression of cell division in Bacillus subtilis. Mol Microbiol. 2006 Jun;60(6):1364-80. PMID:16796675 doi:http://dx.doi.org/MMI5184
- ↑ Duman R, Ishikawa S, Celik I, Strahl H, Ogasawara N, Troc P, Lowe J, Hamoen LW. Structural and genetic analyses reveal the protein SepF as a new membrane anchor for the Z ring. Proc Natl Acad Sci U S A. 2013 Nov 11. PMID:24218584 doi:http://dx.doi.org/10.1073/pnas.1313978110
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