The three-dimensional structure of canine parvovirus and its functional implications

Science ◽  
1991 ◽  
Vol 251 (5000) ◽  
pp. 1456-1464 ◽  
Author(s):  
J Tsao ◽  
M. Chapman ◽  
M Agbandje ◽  
W Keller ◽  
K Smith ◽  
...  
Keyword(s):  
Three Dimensional ◽  
Canine Parvovirus ◽  
Dimensional Structure ◽  
Three Dimensional Structure ◽  
Functional Implications

The Three-Dimensional Structure of Canine Parvovirus and Its Functional Implications

2014 ◽  
pp. 230-238
Author(s):  
Jun Tsao ◽  
Michael S. Chapman ◽  
Mavis Agbandje ◽  
Walter Keller ◽  
Kathy Smith ◽  
...  
Keyword(s):  
Three Dimensional ◽  
Canine Parvovirus ◽  
Dimensional Structure ◽  
Three Dimensional Structure ◽  
Functional Implications

The three-dimensional structure of an eukaryotic glutamine synthetase: Functional implications of its oligomeric structure

2006 ◽  
Vol 156 (3) ◽  
pp. 469-479 ◽  
Author(s):  
Oscar Llorca ◽  
Marco Betti ◽  
José M. González ◽  
Alfonso Valencia ◽  
Antonio J. Márquez ◽  
...  
Keyword(s):  
Glutamine Synthetase ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Oligomeric Structure ◽  
Three Dimensional Structure ◽  
Functional Implications

scholarly journals A Rare Deletion in SARS-CoV-2 ORF6 Dramatically Alters the Predicted Three-Dimensional Structure of the Resultant Protein

2020 ◽  
Author(s):  
Marco A. Riojas ◽  
Andrew M. Frank ◽  
Nikhita P. Puthuveetil ◽  
Beth Flores ◽  
Michael Parker ◽  
...  
Keyword(s):  
Selective Pressure ◽  
Type I Interferon ◽  
Clinical Sample ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Type I ◽  
Three Dimensional Structure ◽  
Clinical Patient ◽  
N Terminus ◽  
Functional Implications

AbstractThe function of the SARS-CoV-2 accessory protein p6, encoded by ORF6, is not fully known. Based upon its similarity to p6 from SARS-CoV, it may play a similar role, namely as an antagonist of type I interferon (IFN) signaling. Here we report the sequencing of a SARS-CoV-2 strain passaged six times after original isolation from a clinical patient in Hong Kong. The genome sequence shows a 27 nt in-frame deletion (Δ27,264-27,290) within ORF6, predicted to result in a 9 aa deletion (ΔFKVSIWNLD) from the central portion of p6. This deletion is predicted to result in a dramatic alteration in the three-dimensional structure of the resultant protein (p6Δ22-30), possibly with significant functional implications. Analysis of the original clinical sample indicates that the deletion was not present, while sequencing of subsequent passages of the strain identifies the deletion as a majority variant. This suggests that the deletion originated ab initio during passaging and subsequently propagated into the majority, possibly due to the removal of selective pressure through the IFN-deficient Vero E6 cell line. The specific function of the SARS-CoV-2 p6 N-terminus, if any, has not yet been determined. However, this deletion is predicted to cause a shift from N-endo to N-ecto in the transmembrane localization of the SARS-CoV-2 p6Δ22-30 N-terminus, possibly leading to the ablation of its native function.

Functional implications of interleukin-1β based on the three-dimensional structure

1992 ◽  
Vol 12 (1) ◽  
pp. 10-23 ◽  
Author(s):  
B. Veerapandian ◽  
Gary L. Gilliland ◽  
Reetta Raag ◽  
Anders L. Svensson ◽  
Yoshihiro Masui ◽  
...  
Keyword(s):  
Three Dimensional ◽  
Interleukin 1Β ◽  
Dimensional Structure ◽  
Three Dimensional Structure ◽  
Functional Implications

The Three-dimensional structure of frozen-hydrated nudaurelia capensis β virus

1987 ◽  
Vol 45 ◽  
pp. 650-651
Author(s):  
N. H. Olson ◽  
T. S. Baker ◽  
Wu Bo Mu ◽  
J. E. Johnson ◽  
D. A. Hendry
Keyword(s):  
South African ◽  
Rna Virus ◽  
Carbon Film ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Electron Dose ◽  
Total Electron ◽  
Three Dimensional Structure ◽  
Negative Stain ◽  
Dimensional Reconstruction

Nudaurelia capensis β virus (NβV) is an RNA virus of the South African Pine Emperor moth, Nudaurelia cytherea capensis (Lepidoptera: Saturniidae). The NβV capsid is a T = 4 icosahedron that contains 60T = 240 subunits of the coat protein (Mr = 61,000). A three-dimensional reconstruction of the NβV capsid was previously computed from visions embedded in negative stain suspended over holes in a carbon film. We have re-examined the three-dimensional structure of NβV, using cryo-microscopy to examine the native, unstained structure of the virion and to provide a initial phasing model for high-resolution x-ray crystallographic studiesNβV was purified and prepared for cryo-microscopy as described. Micrographs were recorded ∼1 - 2 μm underfocus at a magnification of 49,000X with a total electron dose of about 1800 e-/nm2.

Three Dimensional structure and organization of diploid chromosomes by optical section microscopy

1987 ◽  
Vol 45 ◽  
pp. 633-635
Author(s):  
David A. Agard ◽  
Yasushi Hiraoka ◽  
John W. Sedat
Keyword(s):  
Dimensional Space ◽  
Three Dimensional ◽  
Developmental State ◽  
Mitotic Cell ◽  
Biological Properties ◽  
Dimensional Structure ◽  
Specific Gene ◽  
Three Dimensional Structure ◽  
Complementary Techniques ◽  
Dynamic Structures

In an effort to understand the complex relationship between structure and biological function within the nucleus, we have embarked on a program to examine the three-dimensional structure and organization of Drosophila melanogaster embryonic chromosomes. Our overall goal is to determine how DNA and proteins are organized into complex and highly dynamic structures (chromosomes) and how these chromosomes are arranged in three dimensional space within the cell nucleus. Futher, we hope to be able to correlate structual data with such fundamental biological properties as stage in the mitotic cell cycle, developmental state and transcription at specific gene loci.Towards this end, we have been developing methodologies for the three-dimensional analysis of non-crystalline biological specimens using optical and electron microscopy. We feel that the combination of these two complementary techniques allows an unprecedented look at the structural organization of cellular components ranging in size from 100A to 100 microns.

Three-Dimensional Structure of Cloned T3 Connector Protein at 1.6nm Resolution

1990 ◽  
Vol 48 (1) ◽  
pp. 282-283
Author(s):  
José L. Carrascosa ◽  
José M. Valpuesta ◽  
Hisao Fujisawa
Keyword(s):  
Dna Sequences ◽  
Expression Vector ◽  
Three Dimensional ◽  
Deae Cellulose ◽  
Dna Packaging ◽  
Dimensional Structure ◽  
Two Dimensional ◽  
Freezing And Thawing ◽  
Three Dimensional Structure ◽  
Dimensional Reconstruction

The head to tail connector of bacteriophages plays a fundamental role in the assembly of viral heads and DNA packaging. In spite of the absence of sequence homology, the structure of connectors from different viruses (T4, Ø29, T3, P22, etc) share common morphological features, that are most clearly revealed in their three-dimensional structure. We have studied the three-dimensional reconstruction of the connector protein from phage T3 (gp 8) from tilted view of two dimensional crystals obtained from this protein after cloning and purification.DNA sequences including gene 8 from phage T3 were cloned, into Bam Hl-Eco Rl sites down stream of lambda promotor PL, in the expression vector pNT45 under the control of cI857. E R204 (pNT89) cells were incubated at 42°C for 2h, harvested and resuspended in 20 mM Tris HC1 (pH 7.4), 7mM 2 mercaptoethanol, ImM EDTA. The cells were lysed by freezing and thawing in the presence of lysozyme (lmg/ml) and ligthly sonicated. The low speed supernatant was precipitated by ammonium sulfate (60% saturated) and dissolved in the original buffer to be subjected to gel nitration through Sepharose 6B, followed by phosphocellulose colum (Pll) and DEAE cellulose colum (DE52). Purified gp8 appeared at 0.3M NaCl and formed crystals when its concentration increased above 1.5 mg/ml.

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