6e3c
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==NMR Solution Structure of the Monomeric Form of the Phage L Decoration Protein== | |
| + | <StructureSection load='6e3c' size='340' side='right'caption='[[6e3c]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6e3c]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterobacteria_phage_L Enterobacteria phage L]. 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 [https://proteopedia.org/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'>[https://proteopedia.org/fgij/fg.htm?mol=6e3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e3c OCA], [https://pdbe.org/6e3c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6e3c RCSB], [https://www.ebi.ac.uk/pdbsum/6e3c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6e3c ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q5C838_9CAUD Q5C838_9CAUD] | ||
| + | <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: Enterobacteria phage L]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Alexandrescu AT]] | ||
| + | [[Category: Newcomer RL]] | ||
| + | [[Category: Teschke CM]] | ||
Current revision
NMR Solution Structure of the Monomeric Form of the Phage L Decoration Protein
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