View source for 4xcq


==Clostridium botulinum phage c-st TubZ (C-terminal tail truncated protein)==
<StructureSection load='4xcq' size='340' side='right'caption='[[4xcq]], [[Resolution|resolution]] 2.39&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4xcq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_phage_c-st Clostridium phage c-st]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XCQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XCQ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.39&#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=NA:SODIUM+ION'>NA</scene></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=4xcq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xcq OCA], [https://pdbe.org/4xcq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xcq RCSB], [https://www.ebi.ac.uk/pdbsum/4xcq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xcq ProSAT]</span></td></tr>
</table>
== Function ==
[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> 
== References ==
<references/>
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</StructureSection>
[[Category: Clostridium phage c-st]]
[[Category: Large Structures]]
[[Category: Oliva MA]]