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| | <StructureSection load='4p1m' size='340' side='right'caption='[[4p1m]], [[Resolution|resolution]] 1.95Å' scene=''> | | <StructureSection load='4p1m' size='340' side='right'caption='[[4p1m]], [[Resolution|resolution]] 1.95Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4p1m]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P1M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4P1M FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4p1m]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P1M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4P1M FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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]] 1.95Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">zapA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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=4p1m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p1m OCA], [http://pdbe.org/4p1m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4p1m RCSB], [http://www.ebi.ac.uk/pdbsum/4p1m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4p1m 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=4p1m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p1m OCA], [https://pdbe.org/4p1m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4p1m RCSB], [https://www.ebi.ac.uk/pdbsum/4p1m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4p1m ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ZAPA_ECOLX ZAPA_ECOLX]] Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division (By similarity). | + | [https://www.uniprot.org/uniprot/ZAPA_ECOLI ZAPA_ECOLI] Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division.<ref>PMID:15060045</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: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Khursigara, C M]] | + | [[Category: Khursigara CM]] |
| - | [[Category: Kimber, M S]] | + | [[Category: Kimber MS]] |
| - | [[Category: Roach, E J]] | + | [[Category: Roach EJ]] |
| - | [[Category: Cell cycle]]
| + | |
| - | [[Category: Cell division]]
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| - | [[Category: Coiled-coil]]
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| - | [[Category: Ftsz filament bundling]]
| + | |
| Structural highlights
Function
ZAPA_ECOLI Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division.[1]
Publication Abstract from PubMed
FtsZ is an essential cell division protein in Escherichia coli and its localization, filamentation and bundling at the mid-cell are required for Z-ring stability. Once assembled, the Z-ring recruits a series of proteins that comprise the bacterial divisome. FtsZ- associated proteins (Zaps) stabilize the Z-ring by increasing lateral interactions between individual filaments, bundling FtsZ to provide a scaffold for divisome assembly. The X-ray crystallographic structure of E. coli ZapA (EcZapA) was determined, identifying key structural differences from the existing ZapA structure from Pseudomonas aeruginosa, including a charged alpha-helix on the globular domains of the ZapA tetramer. Key helix residues in EcZapA were modified using site- directed mutagenesis. These ZapA variants significantly decreased FtsZ bundling in protein sedimentation assays when compared to wild-type (WT) ZapA proteins. Electron micrographs of ZapA-bundled FtsZ filaments showed the modified ZapA variants altered the number of FtsZ filaments per bundle. These in vitro results were corroborated in vivo by expressing the ZapA variants in an E. coli zapA strain. In vivo, ZapA variants that altered FtsZ bundling showed an elongated phenotype, indicating improper cell division. Our findings highlight the importance of key ZapA residues that influence the extent of FtsZ bundling, and which ultimately affect Z-ring formation in dividing cells.
Crystal structure and site-directed mutational analysis reveals key residues involved in Escherichia coli ZapA function.,Roach EJ, Kimber MS, Khursigara CM J Biol Chem. 2014 Jul 7. pii: jbc.M114.561928. PMID:25002581[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Johnson JE, Lackner LL, Hale CA, de Boer PA. ZipA is required for targeting of DMinC/DicB, but not DMinC/MinD, complexes to septal ring assemblies in Escherichia coli. J Bacteriol. 2004 Apr;186(8):2418-29. PMID:15060045
- ↑ Roach EJ, Kimber MS, Khursigara CM. Crystal structure and site-directed mutational analysis reveals key residues involved in Escherichia coli ZapA function. J Biol Chem. 2014 Jul 7. pii: jbc.M114.561928. PMID:25002581 doi:http://dx.doi.org/10.1074/jbc.M114.561928
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