3m89

From Proteopedia

(Difference between revisions)

Revision as of 08:49, 6 September 2023

Structure of TubZ-GTP-g-S

Structural highlights

3m89 is a 1 chain structure with sequence from Bacillus thuringiensis serovar israelensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TUBZ_BACTI A tubulin-like, filament forming GTPase; the motor component of the type III plasmid partition system which ensures correct segregation of the pBtoxis plasmid. Filaments may seed from the centromere-like site (tubC) when bound by DNA-binding protein TubR; the tubC-TubR complex stabilizes the TubZ filament. 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 (PubMed:20534443, PubMed:23010931, PubMed:25825718). Required for pBtoxis plasmid replication/partition (PubMed:16936050, PubMed:17873046). Binds the TubR-tubC complex; GTP is not required for binding to TubR-tubC. TubZ alone does not bind DNA (PubMed:17873046, PubMed:20534443, PubMed:25825718). Has a high GTPase activity in the presence of Mg(2+); in the presence of GTP assembles into dynamic filaments which upon polymerization bind almost exclusively GDP. Filament formation is cooperative, requiring a critical concentration. Formation occurs very quickly and is followed by disassembly as GTP is consumed (PubMed:18198178).^[1] ^[2] ^[3] ^[4] ^[5] ^[6]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The segregation of plasmid DNA typically requires three elements: a DNA centromere site, an NTPase, and a centromere-binding protein. Because of their simplicity, plasmid partition systems represent tractable models to study the molecular basis of DNA segregation. Unlike eukaryotes, which utilize the GTPase tubulin to segregate DNA, the most common plasmid-encoded NTPases contain Walker-box and actin-like folds. Recently, a plasmid stability cassette on Bacillus thuringiensis pBtoxis encoding a putative FtsZ/tubulin-like NTPase called TubZ and DNA-binding protein called TubR has been described. How these proteins collaborate to impart plasmid stability, however, is unknown. Here we show that the TubR structure consists of an intertwined dimer with a winged helix-turn-helix (HTH) motif. Strikingly, however, the TubR recognition helices mediate dimerization, making canonical HTH-DNA interactions impossible. Mutagenesis data indicate that a basic patch, encompassing the two wing regions and the N termini of the recognition helices, mediates DNA binding, which indicates an unusual HTH-DNA interaction mode in which the N termini of the recognition helices insert into a single DNA groove and the wings into adjacent DNA grooves. The TubZ structure shows that it is as similar structurally to eukaryotic tubulin as it is to bacterial FtsZ. TubZ forms polymers with guanine nucleotide-binding characteristics and polymer dynamics similar to tubulin. Finally, we show that the exposed TubZ C-terminal region interacts with TubR-DNA, linking the TubR-bound pBtoxis to TubZ polymerization. The combined data suggest a mechanism for TubZ-polymer powered plasmid movement.

Plasmid protein TubR uses a distinct mode of HTH-DNA binding and recruits the prokaryotic tubulin homolog TubZ to effect DNA partition.,Ni L, Xu W, Kumaraswami M, Schumacher MA Proc Natl Acad Sci U S A. 2010 Jun 4. PMID:20534443^[7]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Tang M, Bideshi DK, Park HW, Federici BA. Minireplicon from pBtoxis of Bacillus thuringiensis subsp. israelensis. Appl Environ Microbiol. 2006 Nov;72(11):6948-54. PMID:16936050 doi:10.1128/AEM.00976-06
↑ Tang M, Bideshi DK, Park HW, Federici BA. Iteron-binding ORF157 and FtsZ-like ORF156 proteins encoded by pBtoxis play a role in its replication in Bacillus thuringiensis subsp. israelensis. J Bacteriol. 2007 Nov;189(22):8053-8. PMID:17873046 doi:10.1128/JB.00908-07
↑ Chen Y, Erickson HP. In vitro assembly studies of FtsZ/tubulin-like proteins (TubZ) from Bacillus plasmids: evidence for a capping mechanism. J Biol Chem. 2008 Mar 28;283(13):8102-9. PMID:18198178 doi:10.1074/jbc.M709163200
↑ Ni L, Xu W, Kumaraswami M, Schumacher MA. Plasmid protein TubR uses a distinct mode of HTH-DNA binding and recruits the prokaryotic tubulin homolog TubZ to effect DNA partition. Proc Natl Acad Sci U S A. 2010 Jun 4. PMID:20534443
↑ Aylett CH, Lowe J. Superstructure of the centromeric complex of TubZRC plasmid partitioning systems. Proc Natl Acad Sci U S A. 2012 Oct 9;109(41):16522-7. doi:, 10.1073/pnas.1210899109. Epub 2012 Sep 25. PMID:23010931 doi:http://dx.doi.org/10.1073/pnas.1210899109
↑ Fink G, Löwe J. Reconstitution of a prokaryotic minus end-tracking system using TubRC centromeric complexes and tubulin-like protein TubZ filaments. Proc Natl Acad Sci U S A. 2015 Apr 14;112(15):E1845-50. PMID:25825718 doi:10.1073/pnas.1423746112
↑ Ni L, Xu W, Kumaraswami M, Schumacher MA. Plasmid protein TubR uses a distinct mode of HTH-DNA binding and recruits the prokaryotic tubulin homolog TubZ to effect DNA partition. Proc Natl Acad Sci U S A. 2010 Jun 4. PMID:20534443

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3m89"

Categories: Bacillus thuringiensis serovar israelensis | Large Structures | Ni L | Schumacher MA | Xu W

@@ Line 1: / Line 1: @@
 ==Structure of TubZ-GTP-g-S==
-<StructureSection load='3m89' size='340' side='right' caption='[[3m89]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+<StructureSection load='3m89' size='340' side='right'caption='[[3m89]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3m89]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacti Bacti]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M89 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3M89 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3m89]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_thuringiensis_serovar_israelensis Bacillus thuringiensis serovar israelensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M89 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M89 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GSP:5-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE'>GSP</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]] 2&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GSP:5-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE'>GSP</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">B. Thuringeneisis, pBt156 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1430 BACTI])</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=3m89 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m89 OCA], [https://pdbe.org/3m89 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3m89 RCSB], [https://www.ebi.ac.uk/pdbsum/3m89 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3m89 ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3m89 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m89 OCA], [http://pdbe.org/3m89 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3m89 RCSB], [http://www.ebi.ac.uk/pdbsum/3m89 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3m89 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/TUBZ_BACTI TUBZ_BACTI] A tubulin-like, filament forming GTPase; the motor component of the type III plasmid partition system which ensures correct segregation of the pBtoxis plasmid. Filaments may seed from the centromere-like site (tubC) when bound by DNA-binding protein TubR; the tubC-TubR complex stabilizes the TubZ filament. 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 (PubMed:20534443, PubMed:23010931, PubMed:25825718). Required for pBtoxis plasmid replication/partition (PubMed:16936050, PubMed:17873046). Binds the TubR-tubC complex; GTP is not required for binding to TubR-tubC. TubZ alone does not bind DNA (PubMed:17873046, PubMed:20534443, PubMed:25825718). Has a high GTPase activity in the presence of Mg(2+); in the presence of GTP assembles into dynamic filaments which upon polymerization bind almost exclusively GDP. Filament formation is cooperative, requiring a critical concentration. Formation occurs very quickly and is followed by disassembly as GTP is consumed (PubMed:18198178).<ref>PMID:16936050</ref> <ref>PMID:17873046</ref> <ref>PMID:18198178</ref> <ref>PMID:20534443</ref> <ref>PMID:23010931</ref> <ref>PMID:25825718</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 32: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Bacti]]
+[[Category: Bacillus thuringiensis serovar israelensis]]
-[[Category: Ni, L]]
+[[Category: Large Structures]]
-[[Category: Schumacher, M A]]
+[[Category: Ni L]]
-[[Category: Xu, W]]
+[[Category: Schumacher MA]]
-[[Category: Ftsz]]
+[[Category: Xu W]]
-[[Category: Gtp-binding]]
-[[Category: Nucleotide-binding]]
-[[Category: Partition]]
-[[Category: Structural protein]]
-[[Category: Tubulin]]
-[[Category: Tubz]]

3m89

From Proteopedia

Revision as of 08:49, 6 September 2023

Structure of TubZ-GTP-g-S

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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