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| | <StructureSection load='2xka' size='340' side='right'caption='[[2xka]], [[Resolution|resolution]] 3.00Å' scene=''> | | <StructureSection load='2xka' size='340' side='right'caption='[[2xka]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2xka]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacti Bacti]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XKA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XKA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2xka]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_thuringiensis_serovar_israelensis Bacillus thuringiensis serovar israelensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XKA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XKA FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GSP:5-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE'>GSP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2xkb|2xkb]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GSP:5-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE'>GSP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=2xka FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xka OCA], [https://pdbe.org/2xka PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xka RCSB], [https://www.ebi.ac.uk/pdbsum/2xka PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xka 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=2xka FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xka OCA], [https://pdbe.org/2xka PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xka RCSB], [https://www.ebi.ac.uk/pdbsum/2xka PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xka ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/TUBZ_BACTI TUBZ_BACTI] A tubulin-like, filament forming GTPase; the motor component of the type III plasmid partition system which ensures correct segregation of the pBtoxis plasmid. Filaments may seed from the centromere-like site (tubC) when bound by DNA-binding protein TubR; the tubC-TubR complex stabilizes the TubZ filament. Filaments grow at the plus end and depolymerize at the minus end, a process called treadmilling. TubR-tubC complexes track the depolymerizing minus end of the filament, probably pulling plasmid within the cell (PubMed:20534443, PubMed:23010931, PubMed:25825718). Required for pBtoxis plasmid replication/partition (PubMed:16936050, PubMed:17873046). Binds the TubR-tubC complex; GTP is not required for binding to TubR-tubC. TubZ alone does not bind DNA (PubMed:17873046, PubMed:20534443, PubMed:25825718). Has a high GTPase activity in the presence of Mg(2+); in the presence of GTP assembles into dynamic filaments which upon polymerization bind almost exclusively GDP. Filament formation is cooperative, requiring a critical concentration. Formation occurs very quickly and is followed by disassembly as GTP is consumed (PubMed:18198178).<ref>PMID:16936050</ref> <ref>PMID:17873046</ref> <ref>PMID:18198178</ref> <ref>PMID:20534443</ref> <ref>PMID:23010931</ref> <ref>PMID:25825718</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: Bacti]] | + | [[Category: Bacillus thuringiensis serovar israelensis]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Aylett, C H.S]] | + | [[Category: Aylett CHS]] |
| - | [[Category: Lowe, J]] | + | [[Category: Lowe J]] |
| - | [[Category: Cytomotive]]
| + | |
| - | [[Category: Cytoskeleton]]
| + | |
| - | [[Category: Dna segregation]]
| + | |
| - | [[Category: Microtubule]]
| + | |
| - | [[Category: Motor protein]]
| + | |
| - | [[Category: Pbt156]]
| + | |
| - | [[Category: Pbtoxis]]
| + | |
| - | [[Category: Repx]]
| + | |
| - | [[Category: Structural protein]]
| + | |
| - | [[Category: Tubr]]
| + | |
| Structural highlights
Function
TUBZ_BACTI A tubulin-like, filament forming GTPase; the motor component of the type III plasmid partition system which ensures correct segregation of the pBtoxis plasmid. Filaments may seed from the centromere-like site (tubC) when bound by DNA-binding protein TubR; the tubC-TubR complex stabilizes the TubZ filament. Filaments grow at the plus end and depolymerize at the minus end, a process called treadmilling. TubR-tubC complexes track the depolymerizing minus end of the filament, probably pulling plasmid within the cell (PubMed:20534443, PubMed:23010931, PubMed:25825718). Required for pBtoxis plasmid replication/partition (PubMed:16936050, PubMed:17873046). Binds the TubR-tubC complex; GTP is not required for binding to TubR-tubC. TubZ alone does not bind DNA (PubMed:17873046, PubMed:20534443, PubMed:25825718). Has a high GTPase activity in the presence of Mg(2+); in the presence of GTP assembles into dynamic filaments which upon polymerization bind almost exclusively GDP. Filament formation is cooperative, requiring a critical concentration. Formation occurs very quickly and is followed by disassembly as GTP is consumed (PubMed:18198178).[1] [2] [3] [4] [5] [6]
Publication Abstract from PubMed
Low copy number plasmids often depend on accurate partitioning systems for their continued survival. Generally, such systems consist of a centromere-like region of DNA, a DNA-binding adaptor, and a polymerizing cytomotive filament. Together these components drive newly replicated plasmids to opposite ends of the dividing cell. The Bacillus thuringiensis plasmid pBToxis relies on a filament of the tubulin/FtsZ-like protein TubZ for its segregation. By combining crystallography and electron microscopy, we have determined the structure of this filament. We explain how GTP hydrolysis weakens the subunit-subunit contact and also shed light on the partitioning of the plasmid-adaptor complex. The double helical superstructure of TubZ filaments is unusual for tubulin-like proteins. Filaments of ParM, the actin-like partitioning protein, are also double helical. We suggest that convergent evolution shapes these different types of cytomotive filaments toward a general mechanism for plasmid separation.
Filament structure of bacterial tubulin homologue TubZ.,Aylett CH, Wang Q, Michie KA, Amos LA, Lowe J Proc Natl Acad Sci U S A. 2010 Oct 25. PMID:20974911[7]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tang M, Bideshi DK, Park HW, Federici BA. Minireplicon from pBtoxis of Bacillus thuringiensis subsp. israelensis. Appl Environ Microbiol. 2006 Nov;72(11):6948-54. PMID:16936050 doi:10.1128/AEM.00976-06
- ↑ Tang M, Bideshi DK, Park HW, Federici BA. Iteron-binding ORF157 and FtsZ-like ORF156 proteins encoded by pBtoxis play a role in its replication in Bacillus thuringiensis subsp. israelensis. J Bacteriol. 2007 Nov;189(22):8053-8. PMID:17873046 doi:10.1128/JB.00908-07
- ↑ Chen Y, Erickson HP. In vitro assembly studies of FtsZ/tubulin-like proteins (TubZ) from Bacillus plasmids: evidence for a capping mechanism. J Biol Chem. 2008 Mar 28;283(13):8102-9. PMID:18198178 doi:10.1074/jbc.M709163200
- ↑ Ni L, Xu W, Kumaraswami M, Schumacher MA. Plasmid protein TubR uses a distinct mode of HTH-DNA binding and recruits the prokaryotic tubulin homolog TubZ to effect DNA partition. Proc Natl Acad Sci U S A. 2010 Jun 4. PMID:20534443
- ↑ Aylett CH, Lowe J. Superstructure of the centromeric complex of TubZRC plasmid partitioning systems. Proc Natl Acad Sci U S A. 2012 Oct 9;109(41):16522-7. doi:, 10.1073/pnas.1210899109. Epub 2012 Sep 25. PMID:23010931 doi:http://dx.doi.org/10.1073/pnas.1210899109
- ↑ Fink G, Löwe J. Reconstitution of a prokaryotic minus end-tracking system using TubRC centromeric complexes and tubulin-like protein TubZ filaments. Proc Natl Acad Sci U S A. 2015 Apr 14;112(15):E1845-50. PMID:25825718 doi:10.1073/pnas.1423746112
- ↑ Aylett CH, Wang Q, Michie KA, Amos LA, Lowe J. Filament structure of bacterial tubulin homologue TubZ. Proc Natl Acad Sci U S A. 2010 Oct 25. PMID:20974911 doi:10.1073/pnas.1010176107
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