2x8k: Difference between revisions
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==Crystal Structure of SPP1 Dit (gp 19.1) Protein, a Paradigm of Hub Adsorption Apparatus in Gram-positive Infecting Phages.== | |||
<StructureSection load='2x8k' size='340' side='right'caption='[[2x8k]], [[Resolution|resolution]] 2.95Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2x8k]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_phage_SPP1 Bacillus phage SPP1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X8K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X8K FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.95Å</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=2x8k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x8k OCA], [https://pdbe.org/2x8k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x8k RCSB], [https://www.ebi.ac.uk/pdbsum/2x8k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x8k ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/DIT_BPSPP DIT_BPSPP] Forms a 40 Angstroms wide channel at the distal tip of the tail. Remains associated to the tail after DNA ejection.<ref>PMID:20843802</ref> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/x8/2x8k_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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=2x8k ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Siphophage SPP1 infects the Gram+ bacterium Bacillus subtilis using its long non-contractile tail and tail-tip. Electron microscopy (EM) previously allowed a low-resolution assignment of most orf products belonging to these regions. We report here the structure of the SPP1 distal tail protein (Dit, gp19.1). The combination of X-ray crystallography, EM and light scattering established that Dit is a back-to-back dimer of hexamers. However, Dit fitting in the virion EM maps was only possible with a hexamer located between the tail-tube and the tail-tip. Structure comparison revealed high similarity between Dit and a central component of lactophage baseplates. Sequence similarity search expanded its relatedness to several phage proteins, suggesting that Dit is a docking platform for the tail adsorption apparatus in Siphoviridae infecting Gram+ bacteria and that its architecture is a paradigm for these hub proteins. Dit structural similarity extends also to non-contractile and contractile phage tail proteins (gpVN and XkdM) as well as to components of the bacterial type 6 secretion system, supporting an evolutionary connection between all these devices. | |||
Crystal structure of bacteriophage SPP1 distal tail protein (GP 19.1): a baseplate hub paradigm in gram+ infecting phages.,Veesler D, Robin G, Lichiere J, Auzat I, Tavares P, Bron P, Campanacci V, Cambillau C J Biol Chem. 2010 Sep 15. PMID:20843802<ref>PMID:20843802</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2x8k" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
< | </StructureSection> | ||
[[Category: Bacillus phage | [[Category: Bacillus phage SPP1]] | ||
[[Category: Auzat | [[Category: Large Structures]] | ||
[[Category: Bron | [[Category: Auzat I]] | ||
[[Category: Cambillau | [[Category: Bron P]] | ||
[[Category: Campanacci | [[Category: Cambillau C]] | ||
[[Category: Lichiere | [[Category: Campanacci V]] | ||
[[Category: Robin | [[Category: Lichiere J]] | ||
[[Category: Tavares | [[Category: Robin G]] | ||
[[Category: Veesler | [[Category: Tavares P]] | ||
[[Category: Veesler D]] | |||
Latest revision as of 13:22, 9 May 2024
Crystal Structure of SPP1 Dit (gp 19.1) Protein, a Paradigm of Hub Adsorption Apparatus in Gram-positive Infecting Phages.Crystal Structure of SPP1 Dit (gp 19.1) Protein, a Paradigm of Hub Adsorption Apparatus in Gram-positive Infecting Phages.
Structural highlights
FunctionDIT_BPSPP Forms a 40 Angstroms wide channel at the distal tip of the tail. Remains associated to the tail after DNA ejection.[1] 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 PubMedSiphophage SPP1 infects the Gram+ bacterium Bacillus subtilis using its long non-contractile tail and tail-tip. Electron microscopy (EM) previously allowed a low-resolution assignment of most orf products belonging to these regions. We report here the structure of the SPP1 distal tail protein (Dit, gp19.1). The combination of X-ray crystallography, EM and light scattering established that Dit is a back-to-back dimer of hexamers. However, Dit fitting in the virion EM maps was only possible with a hexamer located between the tail-tube and the tail-tip. Structure comparison revealed high similarity between Dit and a central component of lactophage baseplates. Sequence similarity search expanded its relatedness to several phage proteins, suggesting that Dit is a docking platform for the tail adsorption apparatus in Siphoviridae infecting Gram+ bacteria and that its architecture is a paradigm for these hub proteins. Dit structural similarity extends also to non-contractile and contractile phage tail proteins (gpVN and XkdM) as well as to components of the bacterial type 6 secretion system, supporting an evolutionary connection between all these devices. Crystal structure of bacteriophage SPP1 distal tail protein (GP 19.1): a baseplate hub paradigm in gram+ infecting phages.,Veesler D, Robin G, Lichiere J, Auzat I, Tavares P, Bron P, Campanacci V, Cambillau C J Biol Chem. 2010 Sep 15. PMID:20843802[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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