2xkb: Difference between revisions

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-{{Seed}}
-[[Image:2xkb.jpg|left|200px]]
-<!--
+==Crystal structure of GDP-form protofilaments of Bacillus thuringiensis serovar israelensis TubZ==
-The line below this paragraph, containing "STRUCTURE_2xkb", creates the "Structure Box" on the page.
+<StructureSection load='2xkb' size='340' side='right'caption='[[2xkb]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2xkb]] is a 12 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=2XKB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XKB FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-{{STRUCTURE_2xkb|  PDB=2xkb  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2xkb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xkb OCA], [https://pdbe.org/2xkb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xkb RCSB], [https://www.ebi.ac.uk/pdbsum/2xkb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xkb ProSAT]</span></td></tr>
+</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;">
+== 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.
-===CRYSTAL STRUCTURE OF GDP-FORM PROTOFILAMENTS OF BACILLUS THURINGIENSIS SEROVAR ISRAELENSIS TUBZ===
+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<ref>PMID:20974911</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_20974911}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 2xkb" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 20974911 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_20974911}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Bacillus thuringiensis serovar israelensis]]
-XKB is a 12 chains structure with sequences from [http://en.wikipedia.org/wiki/Bacillus_thuringiensis Bacillus thuringiensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XKB OCA].
+[[Category: Large Structures]]
+[[Category: Aylett CHS]]
-==Reference==
+[[Category: Lowe J]]
-<ref group="xtra">PMID:20974911</ref><references group="xtra"/>
-[[Category: Bacillus thuringiensis]]
-[[Category: Aylett, C H.S.]]
-[[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]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Nov 10 06:44:58 2010''