3v3t: Difference between revisions

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<StructureSection load='3v3t' size='340' side='right'caption='[[3v3t]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='3v3t' size='340' side='right'caption='[[3v3t]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3v3t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_botulinum_c_str._stockholm Clostridium botulinum c str. stockholm]. 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 [https://proteopedia.org/fgij/fg.htm?mol=3V3T FirstGlance]. <br>
<table><tr><td colspan='2'>[[3v3t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_botulinum_C_str._Stockholm Clostridium botulinum C str. Stockholm]. 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 [https://proteopedia.org/fgij/fg.htm?mol=3V3T FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CBCST_03566 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=929505 Clostridium botulinum C str. Stockholm])</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]] 2.302&#8491;</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=3v3t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v3t OCA], [https://pdbe.org/3v3t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v3t RCSB], [https://www.ebi.ac.uk/pdbsum/3v3t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v3t 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=3v3t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v3t OCA], [https://pdbe.org/3v3t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v3t RCSB], [https://www.ebi.ac.uk/pdbsum/3v3t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v3t ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/TUBZ_CBCP TUBZ_CBCP] A tubulin-like, filament forming GTPase; the motor component of the type III partition system presumably used to ensure correct segregation of this bacteriophage. In the presence of Mg(2+) and GTP (or GTP-gamma-S) assembles into filaments which upon polymerization are almost exclusively bound to GDP. Filament formation is cooperative, requiring a critical concentration. Formation occurs very quickly and is followed by disassembly as GTP is consumed. Unlike its plasmid homolog in B.thuringiensis (AC Q8KNP3) GTP-gamma-S does not alter filament formation (PubMed:22538818, PubMed:28230082). When forced to assemble with GDP instead of GTP it makes much stiffer, thicker filaments (PubMed:28230082). The filaments bind a DNA centromere-like site (tubC)-TubR complex which extends to surround the TubZ filaments (PubMed:22538818). Highly dynamic 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 phage DNA within the cell (By similarity).[UniProtKB:Q8KNP3]<ref>PMID:22538818</ref> <ref>PMID:28230082</ref>  
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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3v3t" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Clostridium botulinum c str. stockholm]]
[[Category: Clostridium botulinum C str. Stockholm]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Oliva, M A]]
[[Category: Oliva MA]]
[[Category: Gtp binding]]
[[Category: Gtpase]]
[[Category: Rossmann fold]]
[[Category: Structural protein]]
[[Category: Tubulin/ftsz related]]
[[Category: Tubz]]

Latest revision as of 13:30, 1 March 2024

Crystal structure of Clostridium botulinum phage c-st TubZCrystal structure of Clostridium botulinum phage c-st TubZ

Structural highlights

3v3t is a 1 chain structure with sequence from Clostridium botulinum C str. Stockholm. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.302Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TUBZ_CBCP A tubulin-like, filament forming GTPase; the motor component of the type III partition system presumably used to ensure correct segregation of this bacteriophage. In the presence of Mg(2+) and GTP (or GTP-gamma-S) assembles into filaments which upon polymerization are almost exclusively bound to GDP. Filament formation is cooperative, requiring a critical concentration. Formation occurs very quickly and is followed by disassembly as GTP is consumed. Unlike its plasmid homolog in B.thuringiensis (AC Q8KNP3) GTP-gamma-S does not alter filament formation (PubMed:22538818, PubMed:28230082). When forced to assemble with GDP instead of GTP it makes much stiffer, thicker filaments (PubMed:28230082). The filaments bind a DNA centromere-like site (tubC)-TubR complex which extends to surround the TubZ filaments (PubMed:22538818). Highly dynamic 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 phage DNA within the cell (By similarity).[UniProtKB:Q8KNP3][1] [2]

See Also

References

  1. ↑ Oliva MA, Martin-Galiano AJ, Sakaguchi Y, Andreu JM. Tubulin homolog TubZ in a phage-encoded partition system. Proc Natl Acad Sci U S A. 2012 Apr 26. PMID:22538818 doi:10.1073/pnas.1121546109
  2. ↑ Fuentes-Pérez ME, Núñez-Ramírez R, Martín-González A, Juan-Rodríguez D, Llorca O, Moreno-Herrero F, Oliva MA. TubZ filament assembly dynamics requires the flexible C-terminal tail. Sci Rep. 2017 Feb 23;7:43342. PMID:28230082 doi:10.1038/srep43342

3v3t, resolution 2.30Å

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