3v3t: Difference between revisions
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[[ | ==Crystal structure of Clostridium botulinum phage c-st TubZ== | ||
<StructureSection load='3v3t' size='340' side='right' caption='[[3v3t]], [[Resolution|resolution]] 2.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3v3t]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Clostridium_botulinum_c Clostridium botulinum c]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V3T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3V3T FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CBCST_03566 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=36828 Clostridium botulinum C])</td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3v3t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v3t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3v3t RCSB], [http://www.ebi.ac.uk/pdbsum/3v3t PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Partition systems are responsible for the process whereby large and essential plasmids are accurately positioned to daughter cells during bacterial division. They are typically made of three components: a centromere-like DNA zone, an adaptor protein, and an assembling protein that is either a Walker-box ATPase (type I) or an actin-like ATPase (type II). A recently described type III segregation system has a tubulin/FtsZ-like protein, called TubZ, for plasmid movement. Here, we present the 2.3 A structure and dynamic assembly of a TubZ tubulin homolog from a bacteriophage and unravel the Clostridium botulinum phage c-st type III partition system. Using biochemical and biophysical approaches, we prove that a gene upstream from tubZ encodes the partner TubR and localize the centromeric region (tubS), both of which are essential for anchoring phage DNA to the motile TubZ filaments. Finally, we describe a conserved fourth component, TubY, which modulates the TubZ-R-S complex interaction. | |||
Tubulin homolog TubZ in a phage-encoded partition system.,Oliva MA, Martin-Galiano AJ, Sakaguchi Y, Andreu JM Proc Natl Acad Sci U S A. 2012 Apr 26. PMID:22538818<ref>PMID:22538818</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | |||
*[[Tubulin|Tubulin]] | |||
== References == | |||
<references/> | |||
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</StructureSection> | |||
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[[Category: Clostridium botulinum c]] | [[Category: Clostridium botulinum c]] | ||
[[Category: Oliva, M A.]] | [[Category: Oliva, M A.]] | ||
Revision as of 09:45, 5 June 2014
Crystal structure of Clostridium botulinum phage c-st TubZCrystal structure of Clostridium botulinum phage c-st TubZ
Structural highlights
Publication Abstract from PubMedPartition systems are responsible for the process whereby large and essential plasmids are accurately positioned to daughter cells during bacterial division. They are typically made of three components: a centromere-like DNA zone, an adaptor protein, and an assembling protein that is either a Walker-box ATPase (type I) or an actin-like ATPase (type II). A recently described type III segregation system has a tubulin/FtsZ-like protein, called TubZ, for plasmid movement. Here, we present the 2.3 A structure and dynamic assembly of a TubZ tubulin homolog from a bacteriophage and unravel the Clostridium botulinum phage c-st type III partition system. Using biochemical and biophysical approaches, we prove that a gene upstream from tubZ encodes the partner TubR and localize the centromeric region (tubS), both of which are essential for anchoring phage DNA to the motile TubZ filaments. Finally, we describe a conserved fourth component, TubY, which modulates the TubZ-R-S complex interaction. Tubulin homolog TubZ in a phage-encoded partition system.,Oliva MA, Martin-Galiano AJ, Sakaguchi Y, Andreu JM Proc Natl Acad Sci U S A. 2012 Apr 26. PMID:22538818[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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