Thermus flavus 5S rRNA with a molecular weight of about 40 kDa was modified at the 5' and 3' ends. Crystals were obtained under earth and microgravity conditions. The best crystals were obtained during NASA space mission STS 94. For the first time, it was possible to collect a complete data set from 5S rRNA crystals to 7.8 A resolution and to assign the space group as R32, with unit-cell parameters a = b = 110.3, c = 387.6 A, alpha = beta = 90, gamma = 120 degrees.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1107/s0907444900001736 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Modulating Enzyme's Conformational Space: Impact of Substrate Binding, Mode Alteration, and Active Site Mutation in DapC, an Aminotransferase Enzyme of Lysine Biosynthetic Pathway.
J Phys Chem B
January 2025
Department of Chemistry, Indian Institute of Technology Kharagpur, Kharagpur 721302, India.
The microbial aminotransferase enzyme DapC is vital for lysine biosynthesis in various Gram-positive bacteria, including . Characterization of the enzyme's conformational dynamics and identifying the key residues for ligand binding are crucial for the development of effective antimicrobials. This study employs atomistic simulations to explore and categorize the dynamics of DapC in comparison to other classes of aminotransferase.
View Article and Find Full Text PDFDeep Learning-Assisted Fluorescence Single-Particle Detection of Fumonisin B Powered by Entropy-Driven Catalysis and Argonaute.
Anal Chem
January 2025
State Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi 214122, China.
Timely and accurate detection of trace mycotoxins in agricultural products and food is significant for ensuring food safety and public health. Herein, a deep learning-assisted and entropy-driven catalysis (EDC)-Argonaute powered fluorescence single-particle aptasensing platform was developed for ultrasensitive detection of fumonisin B (FB) using single-stranded DNA modified with biotin and red fluorescence-encoded microspheres as a signal probe and streptavidin-conjugated magnetic beads as separation carriers. The binding of aptamer with FB releases the trigger sequence to mediate EDC cycle to produce numerous 5'-phosphorylated output sequences, which can be used as the guide DNA to activate downstream Argonaute (Ago) for cleaving the signal probe, resulting in increased number of fluorescence microspheres remaining in the final reaction supernatant after magnetic separation.
View Article and Find Full Text PDFStructure-Function Relationship of the β-Hairpin of HB27 Laccase.
Int J Mol Sci
January 2025
Departamento de Micro y Nanotecnologías, Instituto de Ciencias Aplicadas y Tecnología, Universidad Nacional Autónoma de México, Cto. Exterior S/N, C.U., Coyoacán, Ciudad de México C.P. 04510, Mexico.
Thermus thermophilus HB27 laccase (Tth-Lac) is a thermostable enzyme that contains a β-hairpin (Ala292-Gln307) covering the substrate entrance. We analyzed the role of this β-hairpin in the enzymatic activity of Tth-Lac through three β-hairpin mutants: two variants without the β-hairpin (C1Tth-Lac and C2Tth-Lac) and one with a partially modified β-hairpin (P1Tth-Lac). Enzymatic activity was assayed with different substrates with and without copper.
View Article and Find Full Text PDFCRISPR-Cas-mediated adaptation of Thermus thermophilus HB8 to environmental stress conditions.
Arch Microbiol
January 2025
Department of Molecular Biosciences, Wenner-Gren Institute, Stockholm University, Stockholm, SE 106 91, Sweden.
Bacteria experience a continual array of environmental stresses, necessitating adaptive mechanisms crucial for their survival. Thermophilic bacteria, such as Thermus thermophilus, face constant environmental challenges, particularly high temperatures, which requires robust adaptive mechanisms for survival. Studying these extremophiles provides valuable insights into the intricate molecular and physiological processes used by extremophiles to adapt and survive in harsh environments.
View Article and Find Full Text PDFLoop engineering of enzymes to control their immobilization and ultimately fabricate more efficient heterogeneous biocatalysts.
Protein Sci
February 2025
Center for Cooperative Research in Biomaterials (CIC biomaGUNE), Basque Research and Technology Alliance (BRTA), San Sebastián, Spain.
Enzyme immobilization is indispensable for enhancing enzyme performance in various industrial applications. Typically, enzymes require specific spatial arrangements for optimal functionality, underscoring the importance of correct orientation. Despite well-known N- or C-terminus tailoring techniques, alternatives for achieving orientation control are limited.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!