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| <StructureSection load='4uxv' size='340' side='right'caption='[[4uxv]], [[Resolution|resolution]] 3.96Å' scene=''> | | <StructureSection load='4uxv' size='340' side='right'caption='[[4uxv]], [[Resolution|resolution]] 3.96Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[4uxv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacsu Bacsu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UXV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UXV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4uxv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UXV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UXV FirstGlance]. <br> |
- | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4uy3|4uy3]]</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=4uxv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uxv OCA], [https://pdbe.org/4uxv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4uxv RCSB], [https://www.ebi.ac.uk/pdbsum/4uxv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4uxv ProSAT]</span></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=4uxv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uxv OCA], [http://pdbe.org/4uxv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4uxv RCSB], [http://www.ebi.ac.uk/pdbsum/4uxv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4uxv ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://www.uniprot.org/uniprot/EZRA_BACSU EZRA_BACSU]] Negative regulator of FtsZ ring formation; modulates the frequency and position of FtsZ ring formation. Inhibits FtsZ ring formation at polar sites. Interacts either with FtsZ or with one of its binding partners to promote depolymerization. | + | [https://www.uniprot.org/uniprot/EZRA_BACSU EZRA_BACSU] Negative regulator of FtsZ ring formation; modulates the frequency and position of FtsZ ring formation. Inhibits FtsZ ring formation at polar sites. Interacts either with FtsZ or with one of its binding partners to promote depolymerization. |
| <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: Bacsu]] | + | [[Category: Bacillus subtilis subsp. subtilis str. 168]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Barrett, J R]] | + | [[Category: Barrett JR]] |
- | [[Category: Basle, A]] | + | [[Category: Basle A]] |
- | [[Category: Cleverley, R M]] | + | [[Category: Cleverley RM]] |
- | [[Category: Daniela, R A]] | + | [[Category: Daniela RA]] |
- | [[Category: Dixon, N E]] | + | [[Category: Dixon NE]] |
- | [[Category: Harry, E J]] | + | [[Category: Harry EJ]] |
- | [[Category: Hewitt, L]] | + | [[Category: Hewitt L]] |
- | [[Category: Khai-Bui, N]] | + | [[Category: Khai-Bui N]] |
- | [[Category: Lewis, R J]] | + | [[Category: Lewis RJ]] |
- | [[Category: Oakley, A J]] | + | [[Category: Oakley AJ]] |
- | [[Category: Solovyova, A]] | + | [[Category: Solovyova A]] |
- | [[Category: Vollmer, W]] | + | [[Category: Vollmer W]] |
- | [[Category: Xu, Z]] | + | [[Category: Xu Z]] |
- | [[Category: Cell cycle]]
| + | |
- | [[Category: Cell wall]]
| + | |
- | [[Category: Divisome]]
| + | |
- | [[Category: Ftsz]]
| + | |
- | [[Category: Spectrin]]
| + | |
- | [[Category: Tubulin]]
| + | |
- | [[Category: Z-ring]]
| + | |
| Structural highlights
Function
EZRA_BACSU Negative regulator of FtsZ ring formation; modulates the frequency and position of FtsZ ring formation. Inhibits FtsZ ring formation at polar sites. Interacts either with FtsZ or with one of its binding partners to promote depolymerization.
Publication Abstract from PubMed
Bacterial cell division is facilitated by a molecular machine-the divisome-that assembles at mid-cell in dividing cells. The formation of the cytokinetic Z-ring by the tubulin homologue FtsZ is regulated by several factors, including the divisome component EzrA. Here we describe the structure of the 60-kDa cytoplasmic domain of EzrA, which comprises five linear repeats of an unusual triple helical bundle. The EzrA structure is bent into a semicircle, providing the protein with the potential to interact at both N- and C-termini with adjacent membrane-bound divisome components. We also identify at least two binding sites for FtsZ on EzrA and map regions of EzrA that are responsible for regulating FtsZ assembly. The individual repeats, and their linear organization, are homologous to the spectrin proteins that connect actin filaments to the membrane in eukaryotes, and we thus propose that EzrA is the founding member of the bacterial spectrin family.
Structure and function of a spectrin-like regulator of bacterial cytokinesis.,Cleverley RM, Barrett JR, Basle A, Bui NK, Hewitt L, Solovyova A, Xu ZQ, Daniel RA, Dixon NE, Harry EJ, Oakley AJ, Vollmer W, Lewis RJ Nat Commun. 2014 Nov 18;5:5421. doi: 10.1038/ncomms6421. PMID:25403286[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Cleverley RM, Barrett JR, Basle A, Bui NK, Hewitt L, Solovyova A, Xu ZQ, Daniel RA, Dixon NE, Harry EJ, Oakley AJ, Vollmer W, Lewis RJ. Structure and function of a spectrin-like regulator of bacterial cytokinesis. Nat Commun. 2014 Nov 18;5:5421. doi: 10.1038/ncomms6421. PMID:25403286 doi:http://dx.doi.org/10.1038/ncomms6421
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