6v1i: Difference between revisions

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<SX load='6v1i' size='340' side='right' viewer='molstar' caption='[[6v1i]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
<SX load='6v1i' size='340' side='right' viewer='molstar' caption='[[6v1i]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6v1i]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_phage_p74-26 Thermus phage p74-26]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6V1I OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6V1I FirstGlance]. <br>
<table><tr><td colspan='2'>[[6v1i]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_virus_P74-26 Thermus virus P74-26]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6V1I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6V1I FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">P74p83 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=466052 Thermus phage P74-26])</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.8&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6v1i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6v1i OCA], [http://pdbe.org/6v1i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6v1i RCSB], [http://www.ebi.ac.uk/pdbsum/6v1i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6v1i 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=6v1i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6v1i OCA], [https://pdbe.org/6v1i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6v1i RCSB], [https://www.ebi.ac.uk/pdbsum/6v1i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6v1i ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/A7XXR0_BP742 A7XXR0_BP742]
Tailed bacteriophages use a DNA-packaging motor to encapsulate their genome during viral particle assembly. The small terminase (TerS) component of this DNA-packaging machinery acts as a molecular matchmaker that recognizes both the viral genome and the main motor component, the large terminase (TerL). However, how TerS binds DNA and the TerL protein remains unclear. Here, we identified gp83 of the thermophilic bacteriophage P74-26 as the TerS protein. We found that TerS(P76-26) oligomerizes into a nonamer that binds DNA, stimulates TerL ATPase activity, and inhibits TerL nuclease activity. A cryo-EM structure of TerS(P76-26) revealed that it forms a ring with a wide central pore and radially arrayed helix-turn-helix (HTH) domains. The structure further showed that these HTH domains, which are thought to bind DNA by wrapping the double helix around the ring, are rigidly held in an orientation distinct from that seen in other TerS proteins. This rigid arrangement of the putative DNA-binding domain imposed strong constraints on how TerS(P76-26) can bind DNA. Finally, the TerS(P76-26) structure lacked the conserved C-terminal beta-barrel domain used by other TerS proteins for binding TerL. This suggests that a well-ordered C-terminal beta-barrel domain is not required for TerS(P76-26) to carry out its matchmaking function. Our work highlights a thermophilic system for studying the role of small terminase proteins in viral maturation and presents the structure of TerS(P76-26), revealing key differences between this thermophilic phage and its mesophilic counterparts.
 
A thermophilic phage uses a small terminase protein with a fixed helix-turn-helix geometry.,Hayes JA, Hilbert BJ, Gaubitz C, Stone NP, Kelch BA J Biol Chem. 2020 Feb 3. pii: RA119.012224. doi: 10.1074/jbc.RA119.012224. PMID:32014998<ref>PMID:32014998</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6v1i" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Terminase|Terminase]]
*[[Terminase 3D Structures|Terminase 3D Structures]]
== References ==
<references/>
__TOC__
__TOC__
</SX>
</SX>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Thermus phage p74-26]]
[[Category: Thermus virus P74-26]]
[[Category: Gaubitz, C]]
[[Category: Gaubitz C]]
[[Category: Hayes, J A]]
[[Category: Hayes JA]]
[[Category: Hilbert, B J]]
[[Category: Hilbert BJ]]
[[Category: Kelch, B A]]
[[Category: Kelch BA]]
[[Category: Stone, N P]]
[[Category: Stone NP]]
[[Category: Bacteriophage]]
[[Category: Helix-turn-helix]]
[[Category: Motor]]
[[Category: Small terminase]]
[[Category: Viral protein]]

Latest revision as of 17:35, 6 March 2024

Cryo-EM reconstruction of the thermophilic bacteriophage P74-26 small terminase- symmetricCryo-EM reconstruction of the thermophilic bacteriophage P74-26 small terminase- symmetric

6v1i, resolution 3.80Å

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