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| | <StructureSection load='4czl' size='340' side='right'caption='[[4czl]], [[Resolution|resolution]] 1.60Å' scene=''> | | <StructureSection load='4czl' size='340' side='right'caption='[[4czl]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4czl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cauvi Cauvi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CZL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CZL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4czl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caulobacter_vibrioides Caulobacter vibrioides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CZL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CZL FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cze|4cze]], [[4czf|4czf]], [[4czg|4czg]], [[4czh|4czh]], [[4czi|4czi]], [[4czj|4czj]], [[4czk|4czk]], [[4czm|4czm]]</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=4czl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4czl OCA], [https://pdbe.org/4czl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4czl RCSB], [https://www.ebi.ac.uk/pdbsum/4czl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4czl 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=4czl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4czl OCA], [http://pdbe.org/4czl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4czl RCSB], [http://www.ebi.ac.uk/pdbsum/4czl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4czl ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [[https://www.uniprot.org/uniprot/MREB_CAUVN MREB_CAUVN]] Forms membrane-associated dynamic filaments that are essential for cell shape determination (PubMed:14982627, PubMed:17880425, PubMed:24843005). Acts by regulating cell wall synthesis and cell elongation, and thus cell shape (PubMed:14982627, PubMed:17880425). A feedback loop between cell geometry and MreB localization may maintain elongated cell shape by targeting cell wall growth to regions of negative cell wall curvature (By similarity). Required for mid-cell peptidoglycan synthesis and cell division. Directs the localization of the cytosolic peptidoglycan precursor-synthesizing enzyme MurG (PubMed:17880425). Also required for proper chromosome segregation (PubMed:15707892). Directs the segregation of origin-proximal but not origin-distal loci (PubMed:15707892).[UniProtKB:P0A9X4]<ref>PMID:14982627</ref> <ref>PMID:15707892</ref> <ref>PMID:17880425</ref> <ref>PMID:24843005</ref> <ref>PMID:14982627</ref> |
| | <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: Cauvi]] | + | [[Category: Caulobacter vibrioides]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ent, F van den]]
| + | [[Category: Lowe J]] |
| - | [[Category: Lowe, J]] | + | [[Category: Van den Ent F]] |
| - | [[Category: Bacterial actin]] | + | |
| - | [[Category: Bacterial cytoskeleton]]
| + | |
| - | [[Category: Structural protein]]
| + | |
| Structural highlights
Function
[MREB_CAUVN] Forms membrane-associated dynamic filaments that are essential for cell shape determination (PubMed:14982627, PubMed:17880425, PubMed:24843005). Acts by regulating cell wall synthesis and cell elongation, and thus cell shape (PubMed:14982627, PubMed:17880425). A feedback loop between cell geometry and MreB localization may maintain elongated cell shape by targeting cell wall growth to regions of negative cell wall curvature (By similarity). Required for mid-cell peptidoglycan synthesis and cell division. Directs the localization of the cytosolic peptidoglycan precursor-synthesizing enzyme MurG (PubMed:17880425). Also required for proper chromosome segregation (PubMed:15707892). Directs the segregation of origin-proximal but not origin-distal loci (PubMed:15707892).[UniProtKB:P0A9X4][1] [2] [3] [4] [5]
Publication Abstract from PubMed
Filaments of all actin-like proteins known to date are assembled from pairs of protofilaments that are arranged in a parallel fashion, generating polarity. Here we show that the prokaryotic actin homologue MreB forms pairs of protofilaments that adopt an antiparallel arrangement in vitro and in vivo. We provide an atomic view of antiparallel protofilaments of Caulobacter MreB as apparent from crystal structures. We show that a protofilament doublet is essential for MreB's function in cell shape maintenance and demonstrate by in vivo site-specific cross-linking the antiparallel orientation of MreB protofilaments in E. coli. 3D cryo-EM shows that pairs of protofilaments of Caulobacter MreB tightly bind to membranes. Crystal structures of different nucleotide and polymerisation states of Caulobacter MreB reveal conserved conformational changes accompanying antiparallel filament formation. Finally, the antimicrobial agents A22/MP265 are shown to bind close to the bound nucleotide of MreB, presumably preventing nucleotide hydrolysis and destabilising double protofilaments.
Bacterial actin MreB forms antiparallel double filaments.,Van den Ent F, Izore T, Bharat TA, Johnson CM, Lowe J Elife. 2014 May 2:e02634. doi: 10.7554/eLife.02634. PMID:24843005[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Figge RM, Divakaruni AV, Gober JW. MreB, the cell shape-determining bacterial actin homologue, co-ordinates cell wall morphogenesis in Caulobacter crescentus. Mol Microbiol. 2004 Mar;51(5):1321-32. doi: 10.1111/j.1365-2958.2003.03936.x. PMID:14982627 doi:http://dx.doi.org/10.1111/j.1365-2958.2003.03936.x
- ↑ Gitai Z, Dye NA, Reisenauer A, Wachi M, Shapiro L. MreB actin-mediated segregation of a specific region of a bacterial chromosome. Cell. 2005 Feb 11;120(3):329-41. doi: 10.1016/j.cell.2005.01.007. PMID:15707892 doi:http://dx.doi.org/10.1016/j.cell.2005.01.007
- ↑ Divakaruni AV, Baida C, White CL, Gober JW. The cell shape proteins MreB and MreC control cell morphogenesis by positioning cell wall synthetic complexes. Mol Microbiol. 2007 Oct;66(1):174-88. doi: 10.1111/j.1365-2958.2007.05910.x. PMID:17880425 doi:http://dx.doi.org/10.1111/j.1365-2958.2007.05910.x
- ↑ Van den Ent F, Izore T, Bharat TA, Johnson CM, Lowe J. Bacterial actin MreB forms antiparallel double filaments. Elife. 2014 May 2:e02634. doi: 10.7554/eLife.02634. PMID:24843005 doi:http://dx.doi.org/10.7554/eLife.02634
- ↑ Figge RM, Divakaruni AV, Gober JW. MreB, the cell shape-determining bacterial actin homologue, co-ordinates cell wall morphogenesis in Caulobacter crescentus. Mol Microbiol. 2004 Mar;51(5):1321-32. doi: 10.1111/j.1365-2958.2003.03936.x. PMID:14982627 doi:http://dx.doi.org/10.1111/j.1365-2958.2003.03936.x
- ↑ Van den Ent F, Izore T, Bharat TA, Johnson CM, Lowe J. Bacterial actin MreB forms antiparallel double filaments. Elife. 2014 May 2:e02634. doi: 10.7554/eLife.02634. PMID:24843005 doi:http://dx.doi.org/10.7554/eLife.02634
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