4ei7

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of Bacillus cereus TubZ, GDP-form

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4ei7"

Categories: Bacillus cereus ATCC 10987 | Large Structures | Hayashi I | Hoshino S

@@ Line 4: / Line 4: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[4ei7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus_ATCC_10987 Bacillus cereus ATCC 10987]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EI7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EI7 FirstGlance]. <br>
-</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></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]] 1.9&#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></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=4ei7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ei7 OCA], [https://pdbe.org/4ei7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ei7 RCSB], [https://www.ebi.ac.uk/pdbsum/4ei7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ei7 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/TUBZ_BACC1 TUBZ_BACC1]] A tubulin-like, filament forming GTPase; the motor component of the type III plasmid partition system which ensures correct segregation of the pBc10987 plasmid (Probable). Binds GTP and forms filaments (PubMed:22847006). The filaments seed from a DNA centromere-like site (tubC)-TubR complex which extends to surround the TubZ filaments. 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 plasmid within the cell (By similarity).[UniProtKB:Q8KNP3]<ref>PMID:22847006</ref> <ref>PMID:22847006</ref>
+[https://www.uniprot.org/uniprot/TUBZ_BACC1 TUBZ_BACC1] A tubulin-like, filament forming GTPase; the motor component of the type III plasmid partition system which ensures correct segregation of the pBc10987 plasmid (Probable). Binds GTP and forms filaments (PubMed:22847006). The filaments seed from a DNA centromere-like site (tubC)-TubR complex which extends to surround the TubZ filaments. 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 plasmid within the cell (By similarity).[UniProtKB:Q8KNP3]<ref>PMID:22847006</ref> <ref>PMID:22847006</ref>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Stable maintenance of low-copy-number plasmids requires partitioning (par) systems that consist of a nucleotide hydrolase, a DNA-binding protein, and a cis-acting DNA-binding site. Tubulin/FtsZ-like GTPase TubZ was identified as a partitioning factor of the virulence plasmids pBtoxis and pXO1 in Bacillus thuringiensis and Bacillus anthracis, respectively. TubZ exhibits high GTPase activity and assembles into polymers both in vivo and in vitro, and its ''treadmilling'' movement is required for plasmid stability in the cell. To investigate the molecular mechanism of pXO1 plasmid segregation by TubZ filaments, we determined the crystal structures of Bacillus cereus TubZ in apo-, GDP- and GTPgammaS-bound forms at a resolution of 2.1, 1.9 and 3.3 A, respectively. Interestingly, the slowly hydrolyzable GTP analog GTPgammaS was hydrolyzed to GDP in the crystal. In the post-GTP-hydrolysis state, GDP-Bc-TubZ forms a dimer by the head-to-tail association of individual subunits in the asymmetric unit, which is similar to the protofilament formation of FtsZ and B. thuringiensis TubZ. The M-loop, however, interacts with the nucleotide-binding site of the adjacent subunit and stabilizes the filament structure in a different manner, which indicates that the molecular assembly of the TubZ-related par systems is not stringently conserved. Furthermore, we show that the C-terminal tail of TubZ is required for association with the DNA-binding protein TubR. Using a combination of crystallography, site-directed mutagenesis and biochemical analysis, our results provide the structural basis of the TubZ polymer that may drive DNA segregation.
-Filament formation of FtsZ/tubulin-like protein TubZ from the Bacillus cereus pXO1 plasmid.,Hoshino S, Hayashi I J Biol Chem. 2012 Jul 30. PMID:22847006<ref>PMID:22847006</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4ei7" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4ei7

From Proteopedia

Current revision

Crystal structure of Bacillus cereus TubZ, GDP-form

Structural highlights

Function

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox