2xkb: Difference between revisions
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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 15:53, 22 October 2014
CRYSTAL STRUCTURE OF GDP-FORM PROTOFILAMENTS OF BACILLUS THURINGIENSIS SEROVAR ISRAELENSIS TUBZCRYSTAL STRUCTURE OF GDP-FORM PROTOFILAMENTS OF BACILLUS THURINGIENSIS SEROVAR ISRAELENSIS TUBZ
Structural highlights
Publication Abstract from PubMedLow 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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