3v3t: Difference between revisions
New page: '''Unreleased structure''' The entry 3v3t is ON HOLD Authors: Oliva, M.A. Description: Crystal structure of Clostridium botulinum phage c-st TubZ |
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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 [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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.302Å</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> | |||
== 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> | |||
==See Also== | |||
*[[Cell division protein 3D structures|Cell division protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Clostridium botulinum C str. Stockholm]] | |||
[[Category: Large Structures]] | |||
[[Category: Oliva MA]] | |||
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
FunctionTUBZ_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 AlsoReferences
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