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| | ==NMR Solution Structure of the Monomeric Form of the Phage L Decoration Protein== | | ==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=''> | + | <StructureSection load='6e3c' size='340' side='right'caption='[[6e3c]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6e3c]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacteriophage_l Bacteriophage 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E3C FirstGlance]. <br> | + | <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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dec ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=45441 Bacteriophage L])</td></tr> | + | </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> |
| - | <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> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q5C838_9CAUD Q5C838_9CAUD] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacteriophage l]] | + | [[Category: Enterobacteria phage L]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Alexandrescu, A T]] | + | [[Category: Alexandrescu AT]] |
| - | [[Category: Newcomer, R L]] | + | [[Category: Newcomer RL]] |
| - | [[Category: Teschke, C M]] | + | [[Category: Teschke CM]] |
| - | [[Category: Cementing]]
| + | |
| - | [[Category: Decoration]]
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| - | [[Category: Ob-fold]]
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| - | [[Category: Viral protein]]
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| Structural highlights
Function
Q5C838_9CAUD
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Newcomer RL, Schrad JR, Gilcrease EB, Casjens SR, Feig M, Teschke CM, Alexandrescu AT, Parent KN. The phage L capsid decoration protein has a novel OB-fold and an unusual capsid binding strategy. Elife. 2019 Apr 4;8. pii: 45345. doi: 10.7554/eLife.45345. PMID:30945633 doi:http://dx.doi.org/10.7554/eLife.45345
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