7rfv: Difference between revisions

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'''Unreleased structure'''


The entry 7rfv is ON HOLD
==Tailspike protein 4 (TSP4) from phage CBA120, residues 1-250, obtained in the presence of PEG8000==
<StructureSection load='7rfv' size='340' side='right'caption='[[7rfv]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7rfv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_CBA120 Escherichia virus CBA120]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7RFV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7RFV 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]] 3.2&#8491;</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=7rfv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7rfv OCA], [https://pdbe.org/7rfv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7rfv RCSB], [https://www.ebi.ac.uk/pdbsum/7rfv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7rfv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/G3M192_9CAUD G3M192_9CAUD]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Four tailspike proteins (TSP1-4) of Escherichia coli O157:H7 bacteriophage CBA120 enable infection of multiple hosts. They form a branched complex that attaches to the tail baseplate. Each TSP recognizes a different lipopolysaccharide on the membrane of a different bacterial host. The 335 N-terminal residues of TSP4 promote the assembly of the TSP complex and anchor it to the tail baseplate. The crystal structure of TSP4-N335 reveals a trimeric protein comprising four domains. The baseplate anchor domain (AD) contains an intertwined triple-stranded beta-helix. The ensuing XD1, XD2 and XD3 beta-sheet containing domains mediate the binding of TSP1-3 to TSP4. Each of the XD domains adopts the same fold as the respective XD domains of bacteriophage T4 gp10 baseplate protein, known to engage in protein-protein interactions via its XD2 and XD3 domains. The structural similarity suggests that XD2 and XD3 of TSP4 also function in protein-protein interactions. Analytical ultracentrifugation analyses of TSP4-N335 and of domain deletion proteins showed how TSP4-N335 promotes the formation of the TSP quaternary complex. TSP1 and TSP2 bind directly to TSP4 whereas TSP3 binding requires a pre-formed TSP4-N335:TSP2 complex. A 3-dimensional model of the bacteriophage CBA120 TSP complex has been developed based on the structural and ultracentrifuge information.


Authors: Chao, K., Shang, X., Grenfield, J., Linden, S.B., Nelson, D.C., Herzberg, O.
Structure of Escherichia coli O157:H7 bacteriophage CBA120 tailspike protein 4 baseplate anchor and tailspike assembly domains (TSP4-N).,Chao KL, Shang X, Greenfield J, Linden SB, Alreja AB, Nelson DC, Herzberg O Sci Rep. 2022 Feb 8;12(1):2061. doi: 10.1038/s41598-022-06073-2. PMID:35136138<ref>PMID:35136138</ref>


Description: Tailspike protein 4 (TSP4) from phage CBA120, residues 1-250, obtained in the presence of PEG8000
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Linden, S.B]]
<div class="pdbe-citations 7rfv" style="background-color:#fffaf0;"></div>
[[Category: Grenfield, J]]
 
[[Category: Chao, K]]
==See Also==
[[Category: Nelson, D.C]]
*[[Tailspike protein|Tailspike protein]]
[[Category: Shang, X]]
== References ==
[[Category: Herzberg, O]]
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia virus CBA120]]
[[Category: Large Structures]]
[[Category: Chao K]]
[[Category: Grenfield J]]
[[Category: Herzberg O]]
[[Category: Linden SB]]
[[Category: Nelson DC]]
[[Category: Shang X]]

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