View source for 5lxl


==NMR structure of the N-terminal domain of the Bacteriophage T5 decoration protein pb10==
<StructureSection load='5lxl' size='340' side='right'caption='[[5lxl]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5lxl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T5 Escherichia virus T5]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LXL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LXL FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=5lxl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lxl OCA], [https://pdbe.org/5lxl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lxl RCSB], [https://www.ebi.ac.uk/pdbsum/5lxl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lxl ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DECO_BPT5 DECO_BPT5] Decoration protein that binds to each capsid protein hexamer after capsid expansion.<ref>PMID:16876823</ref> <ref>PMID:26616586</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bacteriophage capsids constitute icosahedral shells of exceptional stability that protect the viral genome. Many capsids display on their surface decoration proteins whose structure and function remain largely unknown. The decoration protein pb10 of phage T5 binds at the centre of the 120 hexamers formed by the major capsid protein. Here we determined the 3D structure of pb10 and investigated its capsid-binding properties using NMR, SAXS, cryoEM and SPR. Pb10 consists of an alpha-helical capsid-binding domain and an Ig-like domain exposed to the solvent. It binds to the T5 capsid with a remarkably high affinity and its binding kinetics is characterized by a very slow dissociation rate. We propose that the conformational exchange events observed in the capsid-binding domain enable rearrangements upon binding that contribute to the quasi-irreversibility of the pb10-capsid interaction. Moreover we show that pb10 binding is a highly cooperative process, which favours immediate rebinding of newly dissociated pb10 to the 120 hexamers of the capsid protein. In extreme conditions, pb10 protects the phage from releasing its genome. We conclude that pb10 may function to reinforce the capsid thus favouring phage survival in harsh environments.

High affinity anchoring of the decoration protein pb10 onto the bacteriophage T5 capsid.,Vernhes E, Renouard M, Gilquin B, Cuniasse P, Durand D, England P, Hoos S, Huet A, Conway JF, Glukhov A, Ksenzenko V, Jacquet E, Nhiri N, Zinn-Justin S, Boulanger P Sci Rep. 2017 Feb 6;7:41662. doi: 10.1038/srep41662. PMID:28165000<ref>PMID:28165000</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia virus T5]]
[[Category: Large Structures]]
[[Category: Boulanger P]]
[[Category: Cuniasse P]]
[[Category: Gilquin B]]
[[Category: Vernhes E]]
[[Category: Zinn-Justin S]]