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| | <StructureSection load='3zbq' size='340' side='right'caption='[[3zbq]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='3zbq' size='340' side='right'caption='[[3zbq]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3zbq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bpdpk Bpdpk]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZBQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZBQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3zbq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_virus_phiKZ Pseudomonas virus phiKZ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZBQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZBQ 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]] 1.7Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3zbp|3zbp]]</div></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=3zbq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zbq OCA], [https://pdbe.org/3zbq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zbq RCSB], [https://www.ebi.ac.uk/pdbsum/3zbq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zbq 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=3zbq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zbq OCA], [https://pdbe.org/3zbq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zbq RCSB], [https://www.ebi.ac.uk/pdbsum/3zbq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zbq ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/PHUZ_BPDPK PHUZ_BPDPK] A tubulin-like GTPase that forms filaments, which are required for positioning viral DNA and capsids in the middle of the host cell for optimal replication. The motor component of a partition system which pushes phage DNA (encased by protein gp105) to the center of the bacterial host cell (PubMed:28813669). Also required for movement of phage capsids to the vicinity of the viral DNA and rotation of the encased viral DNA at midcell (PubMed:28813669). Forms filaments during the lytic phase, which position phage DNA at the center of the bacterial host cell (PubMed:28813669). Filaments have a three-stranded intertwined architecture and form a spindle-like cytoskeleton within the infected cell (PubMed:23528827). Has GTPase activity (Probable). Filaments grow at the plus end and depolymerize at the minus end, a process called treadmilling, and switch from growing in a polar manner to catastrophic depolymerization, i.e. they display dynamic instability, like tubulin (By similarity). In infected host cells the filament ends close to the cell pole are relatively stable, while the other end near the phage DNA is highly dynamic. Both capsid movement and DNA rotation probably require treadmilling (By similarity).[UniProtKB:B3FK34]<ref>PMID:23528827</ref> <ref>PMID:28813669</ref> <ref>PMID:23528827</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bpdpk]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Aylett, C H.S]] | + | [[Category: Pseudomonas virus phiKZ]] |
| - | [[Category: Lowe, J]] | + | [[Category: Aylett CHS]] |
| - | [[Category: Cytoskeleton]] | + | [[Category: Lowe J]] |
| - | [[Category: Ftsz]]
| + | |
| - | [[Category: Tubulin]]
| + | |
| - | [[Category: Tubz]]
| + | |
| - | [[Category: Viral protein]]
| + | |
| Structural highlights
Function
PHUZ_BPDPK A tubulin-like GTPase that forms filaments, which are required for positioning viral DNA and capsids in the middle of the host cell for optimal replication. The motor component of a partition system which pushes phage DNA (encased by protein gp105) to the center of the bacterial host cell (PubMed:28813669). Also required for movement of phage capsids to the vicinity of the viral DNA and rotation of the encased viral DNA at midcell (PubMed:28813669). Forms filaments during the lytic phase, which position phage DNA at the center of the bacterial host cell (PubMed:28813669). Filaments have a three-stranded intertwined architecture and form a spindle-like cytoskeleton within the infected cell (PubMed:23528827). Has GTPase activity (Probable). Filaments grow at the plus end and depolymerize at the minus end, a process called treadmilling, and switch from growing in a polar manner to catastrophic depolymerization, i.e. they display dynamic instability, like tubulin (By similarity). In infected host cells the filament ends close to the cell pole are relatively stable, while the other end near the phage DNA is highly dynamic. Both capsid movement and DNA rotation probably require treadmilling (By similarity).[UniProtKB:B3FK34][1] [2] [3]
Publication Abstract from PubMed
Pseudomonas PhiKZ-like bacteriophages encode a group of related tubulin/FtsZ-like proteins believed to be essential for the correct centring of replicated bacteriophage virions within the bacterial host. In this study, we present crystal structures of the tubulin/FtsZ-like protein TubZ from Pseudomonas bacteriophage PhiKZ in both the monomeric and protofilament states, revealing that PhiKZ TubZ undergoes structural changes required to polymerise, forming a canonical tubulin/FtsZ-like protofilament. Combining our structures with previous work, we propose a polymerisation-depolymerisation cycle for the Pseudomonas bacteriophage subgroup of tubulin/FtsZ-like proteins. Electron cryo-microscopy of PhiKZ TubZ filaments polymerised in vitro implies a long-pitch helical arrangement for the constituent protofilaments. Intriguingly, this feature is shared by the other known subgroup of bacteriophage tubulin/FtsZ-like proteins from Clostridium species, which are thought to be involved in partitioning the genomes of bacteriophages adopting a pseudo-lysogenic life cycle.
Structure of the Tubulin/FtsZ-Like Protein TubZ from Pseudomonas Bacteriophage PhiKZ.,Aylett CH, Izore T, Amos LA, Lowe J J Mol Biol. 2013 Mar 22. pii: S0022-2836(13)00167-8. doi:, 10.1016/j.jmb.2013.03.019. PMID:23528827[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Aylett CH, Izore T, Amos LA, Lowe J. Structure of the Tubulin/FtsZ-Like Protein TubZ from Pseudomonas Bacteriophage PhiKZ. J Mol Biol. 2013 Mar 22. pii: S0022-2836(13)00167-8. doi:, 10.1016/j.jmb.2013.03.019. PMID:23528827 doi:10.1016/j.jmb.2013.03.019
- ↑ Chaikeeratisak V, Nguyen K, Egan ME, Erb ML, Vavilina A, Pogliano J. The Phage Nucleus and Tubulin Spindle Are Conserved among Large Pseudomonas Phages. Cell Rep. 2017 Aug 15;20(7):1563-1571. doi: 10.1016/j.celrep.2017.07.064. PMID:28813669 doi:http://dx.doi.org/10.1016/j.celrep.2017.07.064
- ↑ Aylett CH, Izore T, Amos LA, Lowe J. Structure of the Tubulin/FtsZ-Like Protein TubZ from Pseudomonas Bacteriophage PhiKZ. J Mol Biol. 2013 Mar 22. pii: S0022-2836(13)00167-8. doi:, 10.1016/j.jmb.2013.03.019. PMID:23528827 doi:10.1016/j.jmb.2013.03.019
- ↑ Aylett CH, Izore T, Amos LA, Lowe J. Structure of the Tubulin/FtsZ-Like Protein TubZ from Pseudomonas Bacteriophage PhiKZ. J Mol Biol. 2013 Mar 22. pii: S0022-2836(13)00167-8. doi:, 10.1016/j.jmb.2013.03.019. PMID:23528827 doi:10.1016/j.jmb.2013.03.019
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