Structure of a hyperthermostable dimeric archaeal Rubisco fromHyperthermus butylicus

2019 ◽  
Vol 75 (6) ◽  
pp. 536-544
Author(s):  
Rudranuj Bundela ◽  
Jeremy Keown ◽  
Serena Watkin ◽  
Frederick Grant Pearce
Keyword(s):  
Crystal Structure ◽  
Thermal Stability ◽  
Electrostatic Interactions ◽  
Thermal Denaturation ◽  
High Thermal Stability ◽  
Enzyme Function ◽  
Oligomeric State ◽  
Bisphosphate Carboxylase ◽  
Hyperthermophilic Archaeon

The crystal structure of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) from the hyperthermophilic archaeonHyperthermus butylicusis presented at 1.8 Å resolution. Previous structures of archaeal Rubisco have been found to assemble into decamers, and this oligomerization was thought to be required for a highly thermally stable enzyme. In the current study,H. butylicusRubisco is shown to exist as a dimer in solution, yet has a thermal denaturation midpoint of 114°C, suggesting that high thermal stability can be achieved without an increased oligomeric state. This increased thermal stability appears to be due to an increased number of electrostatic interactions within the monomeric subunit. As such,H. butylicusRubisco presents a well characterized system in which to investigate the role of assembly and thermal stability in enzyme function.

scholarly journals Crystal Structure Built from a GeO6–GeO5 Polyhedra Network with High Thermal Stability: β–SrGe2O5

2019 ◽  
Vol 1 (10) ◽  
pp. 1989-1993 ◽  
Author(s):  
Christian A. Niedermeier ◽  
Jun-ichi Yamaura ◽  
Jiazhen Wu ◽  
Xinyi He ◽  
Takayoshi Katase ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Thermal Stability ◽  
High Thermal Stability

scholarly journals Structural and Functional Characterization of the Phosphoprotein Central Domain of Spring Viremia of Carp Virus

2020 ◽  
Vol 94 (15) ◽  
Author(s):  
Zhao-Xi Wang ◽  
Shu-Bo Liu ◽  
Hongxin Guan ◽  
Long-Feng Lu ◽  
Jia-Gang Tu ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Functional Characterization ◽  
Oligomeric State ◽  
Hydrophobic Surfaces ◽  
Central Domain ◽  
P Protein ◽  
Homologous Virus ◽  
Β Sheets ◽  
P Proteins

ABSTRACT Spring viremia of carp virus (SVCV) is a highly pathogenic Vesiculovirus in the common carp. The phosphoprotein (P protein) of SVCV is a multifunctional protein that acts as a polymerase cofactor and an antagonist of cellular interferon (IFN) response. Here, we report the 1.5-Å-resolution crystal structure of the P protein central domain (PCD) of SVCV (SVCVPCD). The PCD monomer consists of two β sheets, an α helix, and another two β sheets. Two PCD monomers pack together through their hydrophobic surfaces to form a dimer. The mutations of residues on the hydrophobic surfaces of PCD disrupt the dimer formation to different degrees and affect the expression of host IFN consistently. Therefore, the oligomeric state formation of the P protein of SVCV is an important mechanism to negatively regulate host IFN response. IMPORTANCE SVCV can cause spring viremia of carp with up to 90% lethality, and it is the homologous virus of the notorious vesicular stomatitis virus (VSV). There are currently no drugs that effectively cure this disease. P proteins of negative-strand RNA viruses (NSVs) play an essential role in many steps during the replication cycle and an additional role in immunosuppression as a cofactor. All P proteins of NSVs are oligomeric, but the studies on the role of this oligomerization mainly focus on the process of virus transcription or replication, and there are few studies on the role of PCD in immunosuppression. Here, we present the crystal structure of SVCVPCD. A new mechanism of immune evasion is clarified by exploring the relationship between SVCVPCD and host IFN response from a structural biology point of view. These findings may provide more accurate target sites for drug design against SVCV and provide new insights into the function of NSVPCD.

scholarly journals Influence of electrically neutral nickel atoms on electrical and recombination parameters of silicon

2020 ◽  
Vol 23 (04) ◽  
pp. 361-365
Author(s):  
M.K. Bakhadyrkhanov ◽  
◽  
B.K. Ismaylov ◽  
S.A. Tachilin ◽  
K.A. Ismailov ◽  
...  
Keyword(s):  
Thermal Stability ◽  
Wide Temperature Range ◽  
High Thermal Stability ◽  
Electrical Parameters ◽  
X Ray ◽  
Temperature Range ◽  
Additional Doping ◽  
Thermal Stability Of ◽  
Oxygen Atoms

The results of this study show that creation of clusters from impurity nickel atoms almost completely suppresses generation of thermal donors within the temperature range 450 to 1200 °C. The composition of these clusters was determined using the technique of energy dispersive X-ray spectroscopy, which revealed that the typical cluster consists of silicon atoms (65%), nickel atoms (15%) and oxygen atoms (19%). Based on the experimental results, the authors have suggested that the nickel atoms intensively perform the role of getter for oxygen atoms in the course of clusterization. It was shown that the additional doping of silicon with nickel at T = 1100…1200 °C enables to ensure a sufficiently high thermal stability of its electrical parameters within a wide temperature range.

scholarly journals Lead-free double halide perovskite Cs3BiBr6 with well-defined crystal structure and high thermal stability for optoelectronics

2019 ◽  
Vol 7 (11) ◽  
pp. 3369-3374 ◽  
Author(s):  
Yingying Tang ◽  
Mingli Liang ◽  
Bingdong Chang ◽  
Hongyu Sun ◽  
Kaibo Zheng ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Thermal Stability ◽  
Optoelectronic Devices ◽  
High Thermal Stability ◽  
Lead Free ◽  
Halide Perovskite

A lead-free double-halide perovskite with a well-defined structure was synthesized, likely providing a new candidate material for eco-friendly optoelectronic devices.

Sign in / Sign up

Export Citation Format

Share Document