2fkk: Difference between revisions

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<StructureSection load='2fkk' size='340' side='right'caption='[[2fkk]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
<StructureSection load='2fkk' size='340' side='right'caption='[[2fkk]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2fkk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bpt4 Bpt4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FKK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FKK FirstGlance]. <br>
<table><tr><td colspan='2'>[[2fkk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FKK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FKK FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PO3:PHOSPHITE+ION'>PO3</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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]] 1.2&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2fl8|2fl8]], [[2fl9|2fl9]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PO3:PHOSPHITE+ION'>PO3</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">10 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 BPT4])</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=2fkk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fkk OCA], [https://pdbe.org/2fkk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fkk RCSB], [https://www.ebi.ac.uk/pdbsum/2fkk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fkk 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=2fkk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fkk OCA], [https://pdbe.org/2fkk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fkk RCSB], [https://www.ebi.ac.uk/pdbsum/2fkk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fkk ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/VG10_BPT4 VG10_BPT4]] Structural component of the baseplate.  
[https://www.uniprot.org/uniprot/BP10_BPT4 BP10_BPT4] Baseplate protein that is part of the baseplate wedge and that connects the short tail fibers to the baseplate (PubMed:16554069). During infection, the baseplate undergoes a conformational change from a dome-shaped to a star-shaped structure. At this point, gp10 rotates and acts as a lever that unfolds the short tail fibers, which then interact with host cell surface receptors. Involved in the tail assembly.<ref>PMID:16554069</ref> <ref>PMID:21129200</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2fkk ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2fkk ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The success of tailed bacteriophages to infect cells far exceeds that of most other viruses on account of their specialized tail and associated baseplate structures. The baseplate protein gene product (gp) 10 of bacteriophage T4, whose structure was determined to 1.2 A resolution, was fitted into the cryo-electron microscopy structures of the pre and post-infection conformations of the virus. gp10 functions as a molecular lever that rotates and extends the hinged short tail fibers to facilitate cell attachment. The central folding motif of the gp10 trimer is similar to that of the baseplate protein gp11 and to the receptor-binding domain of the short tail fiber, gp12. The three proteins comprise the periphery of the baseplate and interact with each other. The structural and functional similarities of gp10, gp11, and gp12 and their sequential order in the T4 genome suggest that they evolved separately, subsequent to gene triplication from a common ancestor. Such events are usual in the evolution of complex organelles from a common primordial molecule.
Evolution of bacteriophage tails: Structure of T4 gene product 10.,Leiman PG, Shneider MM, Mesyanzhinov VV, Rossmann MG J Mol Biol. 2006 May 5;358(3):912-21. Epub 2006 Mar 9. PMID:16554069<ref>PMID:16554069</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2fkk" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bpt4]]
[[Category: Escherichia virus T4]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Leiman, P G]]
[[Category: Leiman PG]]
[[Category: Mesyanzhinov, V V]]
[[Category: Mesyanzhinov VV]]
[[Category: Rossmann, M G]]
[[Category: Rossmann MG]]
[[Category: Shneider, M M]]
[[Category: Shneider MM]]
[[Category: Bacteriophage t4]]
[[Category: Baseplate]]
[[Category: Evolution]]
[[Category: Gp10]]
[[Category: Structural comparison]]
[[Category: Tail]]
[[Category: Viral protein]]

Latest revision as of 12:24, 14 February 2024

Crystal structure of the C-terminal domain of the bacteriophage T4 gene product 10Crystal structure of the C-terminal domain of the bacteriophage T4 gene product 10

Structural highlights

2fkk is a 1 chain structure with sequence from Escherichia virus T4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.2Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

BP10_BPT4 Baseplate protein that is part of the baseplate wedge and that connects the short tail fibers to the baseplate (PubMed:16554069). During infection, the baseplate undergoes a conformational change from a dome-shaped to a star-shaped structure. At this point, gp10 rotates and acts as a lever that unfolds the short tail fibers, which then interact with host cell surface receptors. Involved in the tail assembly.[1] [2]

Evolutionary Conservation

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

References

  1. ↑ Leiman PG, Shneider MM, Mesyanzhinov VV, Rossmann MG. Evolution of bacteriophage tails: Structure of T4 gene product 10. J Mol Biol. 2006 May 5;358(3):912-21. Epub 2006 Mar 9. PMID:16554069 doi:10.1016/j.jmb.2006.02.058
  2. ↑ Leiman PG, Arisaka F, van Raaij MJ, Kostyuchenko VA, Aksyuk AA, Kanamaru S, Rossmann MG. Morphogenesis of the T4 tail and tail fibers. Virol J. 2010 Dec 3;7:355. doi: 10.1186/1743-422X-7-355. PMID:21129200 doi:10.1186/1743-422X-7-355

2fkk, resolution 1.20Å

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