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2xkb
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| - | [[ | + | ==CRYSTAL STRUCTURE OF GDP-FORM PROTOFILAMENTS OF BACILLUS THURINGIENSIS SEROVAR ISRAELENSIS TUBZ== |
| + | <StructureSection load='2xkb' size='340' side='right' caption='[[2xkb]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2xkb]] is a 12 chain structure with sequence 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XKB FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</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">[[2xka|2xka]]</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=2xkb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xkb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xkb RCSB], [http://www.ebi.ac.uk/pdbsum/2xkb PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <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. | ||
| - | + | 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | ||
| - | == | + | |
| - | < | + | |
[[Category: Bacillus thuringiensis]] | [[Category: Bacillus thuringiensis]] | ||
[[Category: Aylett, C H.S.]] | [[Category: Aylett, C H.S.]] | ||
Revision as of 12:53, 22 October 2014
CRYSTAL STRUCTURE OF GDP-FORM PROTOFILAMENTS OF BACILLUS THURINGIENSIS SEROVAR ISRAELENSIS TUBZ
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