5l35
From Proteopedia
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<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=5l35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l35 OCA], [http://pdbe.org/5l35 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5l35 RCSB], [http://www.ebi.ac.uk/pdbsum/5l35 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5l35 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=5l35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l35 OCA], [http://pdbe.org/5l35 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5l35 RCSB], [http://www.ebi.ac.uk/pdbsum/5l35 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5l35 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The enormous prevalence of tailed DNA bacteriophages on this planet is enabled by highly efficient self-assembly of hundreds of protein subunits into highly stable capsids. These capsids can stand with an internal pressure as high as approximately 50 atmospheres as a result of the phage DNA-packaging process. Here we report the complete atomic model of the headful DNA-packaging bacteriophage Sf6 at 2.9 A resolution determined by electron cryo-microscopy. The structure reveals the DNA-inflated, tensed state of a robust protein shell assembled via noncovalent interactions. Remarkable global conformational polymorphism of capsid proteins, a network formed by extended N arms, mortise-and-tenon-like intercapsomer joints, and abundant beta-sheet-like mainchain:mainchain intermolecular interactions, confers significant strength yet also flexibility required for capsid assembly and DNA packaging. Differential formations of the hexon and penton are mediated by a drastic alpha-helix-to-beta-strand structural transition. The assembly scheme revealed here may be common among tailed DNA phages and herpesviruses. | ||
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| + | Structure of a headful DNA-packaging bacterial virus at 2.9 A resolution by electron cryo-microscopy.,Zhao H, Li K, Lynn AY, Aron KE, Yu G, Jiang W, Tang L Proc Natl Acad Sci U S A. 2017 Mar 20. pii: 201615025. doi:, 10.1073/pnas.1615025114. PMID:28320961<ref>PMID:28320961</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5l35" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 06:53, 5 April 2017
Cryo-EM structure of bacteriophage Sf6 at 2.9 Angstrom resolution
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Categories: Shigella phage sf6 | Tang, L | Zhao, H | Phage | Sf6 | Virus
