3zig: Difference between revisions
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==SepF-like protein from Pyrococcus furiosus== | |||
=== | <StructureSection load='3zig' size='340' side='right' caption='[[3zig]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3zig]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus_com1 Pyrococcus furiosus com1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZIG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZIG FirstGlance]. <br> | |||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3zie|3zie]], [[3zih|3zih]], [[3zii|3zii]]</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=3zig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zig OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3zig RCSB], [http://www.ebi.ac.uk/pdbsum/3zig PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:24218584</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Pyrococcus furiosus com1]] | [[Category: Pyrococcus furiosus com1]] | ||
[[Category: Celik, I | [[Category: Celik, I]] | ||
[[Category: Duman, R | [[Category: Duman, R]] | ||
[[Category: Hamoen, L W | [[Category: Hamoen, L W]] | ||
[[Category: Ishikawa, S | [[Category: Ishikawa, S]] | ||
[[Category: Lowe, J | [[Category: Lowe, J]] | ||
[[Category: Ogasawara, N | [[Category: Ogasawara, N]] | ||
[[Category: Cell cycle]] | [[Category: Cell cycle]] | ||
Revision as of 20:43, 21 December 2014
SepF-like protein from Pyrococcus furiosusSepF-like protein from Pyrococcus furiosus
Structural highlights
Publication Abstract from PubMedA 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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