6p3e: Difference between revisions

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<SX load='6p3e' size='340' side='right' viewer='molstar' caption='[[6p3e]], [[Resolution|resolution]] 5.40&Aring;' scene=''>
<SX load='6p3e' size='340' side='right' viewer='molstar' caption='[[6p3e]], [[Resolution|resolution]] 5.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6p3e]] is a 18 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacteriophage_lambda Bacteriophage lambda]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6P3E OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6P3E FirstGlance]. <br>
<table><tr><td colspan='2'>[[6p3e]] is a 18 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_Lambda Escherichia virus Lambda]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6P3E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6P3E FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">V, lambdap13 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10710 Bacteriophage lambda])</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]] 5.4&#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=6p3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6p3e OCA], [http://pdbe.org/6p3e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6p3e RCSB], [http://www.ebi.ac.uk/pdbsum/6p3e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6p3e 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=6p3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6p3e OCA], [https://pdbe.org/6p3e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6p3e RCSB], [https://www.ebi.ac.uk/pdbsum/6p3e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6p3e ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/TUBE_LAMBD TUBE_LAMBD]] Forms the phage's tail tube composed of 32 hexameric disks. When it encounters the appropriate initiation complex gpM and gpL, it assembles in hexameric rings that stack on top of each others. Multimerization ceases when the correct tail length is achieved through a mechanism dependent on tail terminator protein.<ref>PMID:2150582</ref> <ref>PMID:23911548</ref> 
[https://www.uniprot.org/uniprot/TUBE_LAMBD TUBE_LAMBD] Forms the phage's tail tube composed of 32 hexameric disks. When it encounters the appropriate initiation complex gpM and gpL, it assembles in hexameric rings that stack on top of each others. Multimerization ceases when the correct tail length is achieved through a mechanism dependent on tail terminator protein.<ref>PMID:2150582</ref> <ref>PMID:23911548</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The long flexible tail tube of bacteriophage lambda connects its capsid to the tail tip. Upon infection, a DNA ejection signal is passed from the tip, along the tube to the capsid that triggers passage of the DNA down the tube and into the host bacterium. The tail tube is built from repeating units of the major tail protein, gpV, which has two distinctive domains. Its N-terminal domain has the same fold as proteins that form the rigid inner tubes of contractile tail phages such as T4 and its C-terminal domain adopt an Ig-like fold of unknown function. We determined structures of the lambda tail tube in free tails and in virions before and after DNA ejection using cryo-electron microscopy. Modeling of the density maps reveals how electrostatic interactions and a mobile loop participate in assembly and also impart flexibility to the tube while maintaining its integrity. We also demonstrate how a common protein fold produces rigid tubes in some phages but flexible tubes in others.
 
Mobile loops and electrostatic interactions maintainthe flexible tail tube of bacteriophage lambda.,Campbell PL, Duda RL, Nassur J, Conway JF, Huet A J Mol Biol. 2019 Nov 8. pii: S0022-2836(19)30647-3. doi:, 10.1016/j.jmb.2019.10.031. PMID:31711962<ref>PMID:31711962</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6p3e" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
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[[Category: Bacteriophage lambda]]
[[Category: Escherichia virus Lambda]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Campbell, P]]
[[Category: Campbell P]]
[[Category: Conway, J F]]
[[Category: Conway JF]]
[[Category: Duda, R L]]
[[Category: Duda RL]]
[[Category: Hendrix, R W]]
[[Category: Hendrix RW]]
[[Category: Huet, A]]
[[Category: Huet A]]
[[Category: Nassur, J]]
[[Category: Nassur J]]
[[Category: Helical]]
[[Category: Siphoviridae]]
[[Category: Tail tube]]
[[Category: Viral protein]]

Latest revision as of 12:25, 20 March 2024

Mobile loops and electrostatic interactions maintain the flexible lambda tail tubeMobile loops and electrostatic interactions maintain the flexible lambda tail tube

6p3e, resolution 5.40Å

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