6e3c: Difference between revisions
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==NMR Solution Structure of the Monomeric Form of the Phage L Decoration Protein== | |||
<StructureSection load='6e3c' size='340' side='right'caption='[[6e3c]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6e3c]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E3C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E3C FirstGlance]. <br> | |||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6e3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e3c OCA], [http://pdbe.org/6e3c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e3c RCSB], [http://www.ebi.ac.uk/pdbsum/6e3c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e3c ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The major coat proteins of dsDNA tailed phages (order Caudovirales) and herpesviruses form capsids by a mechanism that includes active packaging of the dsDNA genome into a precursor procapsid, followed by expansion and stabilization of the capsid. These viruses have evolved diverse strategies to fortify their capsids, such as non-covalent binding of auxiliary 'decoration' (Dec) proteins. The Dec protein from the P22-like phage L has a highly unusual binding strategy that distinguishes between nearly identical three-fold and quasi-three-fold sites of the icosahedral capsid. Cryo-electron microscopy and three-dimensional image reconstruction were employed to determine the structure of native phage L particles. NMR was used to determine the structure/dynamics of Dec in solution. The NMR structure and the cryo-EM density envelope were combined to build a model of the capsid-bound Dec trimer. Key regions that modulate the binding interface were verified by site-directed mutagenesis. | |||
The phage L capsid decoration protein has a novel OB-fold and an unusual capsid binding strategy.,Newcomer RL, Schrad JR, Gilcrease EB, Casjens SR, Feig M, Teschke CM, Alexandrescu AT, Parent KN Elife. 2019 Apr 4;8. pii: 45345. doi: 10.7554/eLife.45345. PMID:30945633<ref>PMID:30945633</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6e3c" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Alexandrescu, A T]] | |||
[[Category: Newcomer, R L]] | |||
[[Category: Teschke, C M]] | |||
[[Category: Cementing]] | |||
[[Category: Decoration]] | |||
[[Category: Ob-fold]] | |||
[[Category: Viral protein]] | |||
Revision as of 05:54, 17 April 2019
NMR Solution Structure of the Monomeric Form of the Phage L Decoration Protein
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