scholarly journals Structure of a headful DNA-packaging bacterial virus at 2.9 Å resolution by electron cryo-microscopy

2017 ◽  
Vol 114 (14) ◽  
pp. 3601-3606 ◽  
Author(s):  
Haiyan Zhao ◽  
Kunpeng Li ◽  
Anna Y. Lynn ◽  
Keith E. Aron ◽  
Guimei Yu ◽  
...  
Keyword(s):  
Self Assembly ◽  
Noncovalent Interactions ◽  
Dna Packaging ◽  
Protein Subunits ◽  
Significant Strength ◽  
Phage Dna ◽  
Mortise And Tenon ◽  
Α Helix ◽  
Β Sheet ◽  
Protein Shell

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 ∼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 Å 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 β-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 α–helix-to-β–strand structural transition. The assembly scheme revealed here may be common among tailed DNA phages and herpesviruses.

scholarly journals Amyloid Self‐Assembly of hIAPP8‐20 via the Accumulation of Helical Oligomers, α‐Helix to β‐Sheet Transition, and Formation of β‐Barrel Intermediates

Small ◽  
2019 ◽  
Vol 15 (18) ◽  
pp. 1805166 ◽  
Author(s):  
Yunxiang Sun ◽  
Aleksandr Kakinen ◽  
Yanting Xing ◽  
Pouya Faridi ◽  
Aparna Nandakumar ◽  
...  
Keyword(s):  
Self Assembly ◽  
Α Helix ◽  
Β Sheet

Stabilization of an α Helix by β-Sheet-Mediated Self-Assembly of a Macrocyclic Peptide

2009 ◽  
Vol 121 (9) ◽  
pp. 1629-1633 ◽  
Author(s):  
Yong-beom Lim ◽  
Kyung-Soo Moon ◽  
Myongsoo Lee
Keyword(s):  
Self Assembly ◽  
Α Helix ◽  
Β Sheet ◽  
Macrocyclic Peptide

Self-Assembly of Recombinant Hagfish Thread Keratins Amenable to a Strain-Induced α-Helix to β-Sheet Transition

2015 ◽  
Vol 16 (8) ◽  
pp. 2327-2339 ◽  
Author(s):  
Jing Fu ◽  
Paul A. Guerette ◽  
Ali Miserez
Keyword(s):  
Self Assembly ◽  
Α Helix ◽  
Β Sheet

Self-assembly and gelation properties of α-helix versus β-sheet forming peptides

Soft Matter ◽  
2009 ◽  
Vol 5 (1) ◽  
pp. 193-202 ◽  
Author(s):  
A. Saiani ◽  
A. Mohammed ◽  
H. Frielinghaus ◽  
R. Collins ◽  
N. Hodson ◽  
...  
Keyword(s):  
Self Assembly ◽  
Sheet Forming ◽  
Α Helix ◽  
Β Sheet

scholarly journals Peptide Self‐Assembly: Amyloid Self‐Assembly of hIAPP8‐20 via the Accumulation of Helical Oligomers, α‐Helix to β‐Sheet Transition, and Formation of β‐Barrel Intermediates (Small 18/2019)

Small ◽  
2019 ◽  
Vol 15 (18) ◽  
pp. 1970093 ◽  
Author(s):  
Yunxiang Sun ◽  
Aleksandr Kakinen ◽  
Yanting Xing ◽  
Pouya Faridi ◽  
Aparna Nandakumar ◽  
...  
Keyword(s):  
Self Assembly ◽  
Α Helix ◽  
Β Sheet

Stabilization of an α Helix by β-Sheet-Mediated Self-Assembly of a Macrocyclic Peptide

2009 ◽  
Vol 48 (9) ◽  
pp. 1601-1605 ◽  
Author(s):  
Yong-beom Lim ◽  
Kyung-Soo Moon ◽  
Myongsoo Lee
Keyword(s):  
Self Assembly ◽  
Α Helix ◽  
Β Sheet ◽  
Macrocyclic Peptide

Structure and assembly of filamentous bacterial viruses

1976 ◽  
Vol 276 (943) ◽  
pp. 81-98 ◽  
Keyword(s):  
Plasma Membrane ◽  
Coat Protein ◽  
Axial Direction ◽  
Early Step ◽  
Circular Dna ◽  
Protein Subunits ◽  
Myosin Filaments ◽  
Bacterial Viruses ◽  
Α Helix ◽  
Protein Shell

Filamentous bacterial viruses are flexible nucleoprotein rods, about 6 nm in diameter by 1000-2000 nm in length (depending on the virus strain). A protein shell encloses a central core of single-stranded circular DNA. The coat protein subunits forming the shell are largely α-helix, elongated in an axial direction, and also sloping radially, so as to overlap each other and give an arrangement of subunits reminiscent of scales on a fish. This arrangement of α-helices is rather like some models of myosin filaments. An early step in assembly of the virion is the formation of a complex between the viral DNA and an intracellular packaging protein that is not found in completed virions. Newly synthesized coat protein becomes associated with the plasma membrane of the cell. During the final steps of assembly, the packaging protein is displaced from the DNA and replaced by coat protein as the virion passes out through the plasma membrane of the host cell.

Scorpion toxin-potassium channel interaction law and its applications.

2020 ◽  
Vol 01 ◽  
Author(s):  
Zheng Zuo ◽  
Zongyun Chen ◽  
Zhijian Cao ◽  
Wenxin Li ◽  
Yingliang Wu
Keyword(s):  
Potassium Channel ◽  
Scorpion Toxin ◽  
Scorpion Toxins ◽  
Toxin Binding ◽  
Channel Interaction ◽  
Binding Interface ◽  
Α Helix ◽  
Interaction Law ◽  
Binding Interfaces ◽  
Β Sheet

: The scorpion toxins are the largest potassium channel-blocking peptide family. The understanding of toxin binding interfaces is usually restricted by two classical binding interfaces: one is the toxin α-helix motif, the other is the antiparallel β-sheet motif. In this review, such traditional knowledge was updated by another two different binding interfaces: one is BmKTX toxin using the turn motif between the α-helix and antiparallel β-sheet domains as the binding interface, the other is Ts toxin using turn motif between the β-sheet in the N-terminal and α-helix domains as the binding interface. Their interaction analysis indicated that the scarce negatively charged residues in the scorpion toxins played a critical role in orientating the toxin binding interface. In view of the toxin negatively charged amino acids as “binding interface regulator”, the law of scorpion toxin-potassium channel interaction was proposed, that is, the polymorphism of negatively charged residue distribution determines the diversity of toxin binding interfaces. Such law was used to develop scorpion toxin-potassium channel recognition control technique. According to this technique, three Kv1.3 channel-targeted peptides, using BmKTX as the template, were designed with the distinct binding interfaces from that of BmKTX through modulating the distribution of toxin negatively charged residues. In view of the potassium channel as the common targets of different animal toxins, the proposed law was also shown to helpfully orientate the binding interfaces of other animal toxins. Clearly, the toxin-potassium channel interaction law would strongly accelerate the research and development of different potassium channelblocking animal toxins in the future.

scholarly journals Dualities in the analysis of phage DNA packaging motors

Bacteriophage ◽  
2012 ◽  
Vol 2 (4) ◽  
pp. e23829 ◽  
Author(s):  
Philip Serwer ◽  
Wen Jiang
Keyword(s):  
Dna Packaging ◽  
Phage Dna
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