A5014390286- RNA and protein synthesis mechanisms
- Enzyme Structure and Function
- Radiative Heat Transfer Studies
- RNA modifications and cancer
- Combustion and flame dynamics
- Thermochemical Biomass Conversion Processes
- Bacterial Genetics and Biotechnology
- RNA Research and Splicing
- Heat transfer and supercritical fluids
- Bacteriophages and microbial interactions
- Embedded Systems Design Techniques
- Protein Structure and Dynamics
- Chaos-based Image/Signal Encryption
- Parallel Computing and Optimization Techniques
- DNA and Nucleic Acid Chemistry
- Metal Extraction and Bioleaching
- Security and Verification in Computing
- Extraction and Separation Processes
- Biochemical and Molecular Research
- Iron and Steelmaking Processes
- DNA Repair Mechanisms
- Metallurgical Processes and Thermodynamics
- Advanced Steganography and Watermarking Techniques
- Smart Grid Security and Resilience
- TGF-β signaling in diseases
Yale University
2009-2024
Anhui University of Technology
2014-2024
Chinese Academy of Agricultural Sciences
2023
University of Science and Technology Beijing
2023
Ministry of Agriculture and Rural Affairs
2023
Academy of Mathematics and Systems Science
2021
Chinese Academy of Sciences
2021
Wuhu Hit Robot Technology Research Institute
2017
Wuhan Institute of Technology
2017
Gwangju Institute of Science and Technology
2015-2017
We have determined the crystal structure of proteolytic component caseinolytic Clp protease (ClpP) from E. coli at 2.3 Å resolution using an ab initio phasing procedure that exploits internal 14-fold symmetry oligomer. The a ClpP monomer has distinct fold defines fifth structural family serine proteases but conserved catalytic apparatus. active resembles hollow, solid-walled cylinder composed two 7-fold symmetric rings stacked back-to-back. Its 14 sites are located within central, roughly...
Isoleucyl-transfer RNA (tRNA) synthetase (IleRS) joins Ile to tRNA(Ile) at its synthetic active site and hydrolyzes incorrectly acylated amino acids editing site. The 2.2 angstrom resolution crystal structure of Staphylococcus aureus IleRS complexed with Mupirocin shows the acceptor strand in continuously stacked, A-form conformation 3' terminal nucleotide To position terminus site, must adopt hairpinned seen tRNA(Gln) synthetase. acid activity may result from incorrect products shuttling...
Article4 September 2015Open Access Structure and function of the N-terminal domain human mitochondrial calcium uniporter Youngjin Lee School Life Sciences, Gwangju Institute Science Technology (GIST), Gwangju, Korea Steitz Center for Structural Biology, Search more papers by this author Choon Kee Min Systems Biology Research Center, Tae Gyun Kim Hong Ki Song Yunki Lim Dongwook Kahee Shin Moonkyung Kang Graduate New Drug Discovery & Development, Chungnam National University, Daejon, Jung Youn...
A recently reported crystal structure of an intact bacterial group I self-splicing intron in complex with both its exons provided the first molecular view into mechanism RNA splicing. This structure, which was trapped state prior to exon ligation reaction, also reveals architecture a fold. The majority is contained within three internally stacked, but sequence discontinuous, helical domains. Here tertiary hydrogen bonding and stacking interactions between domains, single-stranded joiner...
Significance Twister is a small self-cleaving ribozyme similar in size to the hammerhead but uses an orthogonal fold for catalytic rate constant. However, mechanistic source of increase generated by twister was unknown. We present crystal structures from Orzyza sativa as well sequence organism that has not been cultured isolation and identify RNA nucleotides are vital self-cleavage, suggest their roles, update twister’s conserved secondary structure model.
The binding of cAMP to the Escherichia coli catabolite gene activator protein (CAP) produces a conformational change that enables it bind specific DNA sequences and regulate transcription, which cannot do in absence nucleotide. crystal structures unliganded CAP containing D138L mutation WT were determined at 2.3 3.6 A resolution, respectively, reveal two domains have dimerized into one rigid body their recognition helices become buried. structure shows multiple orientations this relative...
Significance Based on the “RNA world” theory, ribozymes likely carried out biochemical reactions long before organisms evolved to use protein enzymes as biocatalysts. The continued discovery of new structures for small self-cleaving has shed light conserved mechanisms in evolution, such acid–base catalysis self-cleavage reaction. Here, we present crystal structure a newly discovered class called Pistol and how it uses phosphoester transfer mechanism self-cleavage. results presented here...
Industrial production of antibiotics, such as semisynthetic penicillins and cephalosporins, requires optically pure d-p-hydroxylphenylglycine its derivatives important side-chain precursors. To produce d-amino acids, microbial d-hydantoinase (E.C. 3.5.2.2) is used for stereospecific hydrolysis chemically synthesized cyclic hydantoins. We report the apo-crystal structure from B. stearothermophilus SD1 at 3.0 Å resolution. The has a classic TIM barrel fold. Despite an undetectable similarity...
The RtcB protein has recently been identified as a 3'-phosphate RNA ligase that directly joins an strand ending with 2',3'-cyclic phosphate to the 5'-hydroxyl group of another in GTP/Mn(2+)-dependent reaction. Here, we report two crystal structures Pyrococcus horikoshii RNA-splicing complex Mn(2+) alone (RtcB/ Mn(2+)) and together covalently bound GMP (RtcB-GMP/Mn(2+)). RtcB/ structure (at 1.6 Å resolution) shows ions at active site, array sulfate nearby indicate binding sites backbone....
Tetratricopeptide repeats (TPRs) are protein domains that mediate key protein-protein interactions in cells. Several TPR bind the C-termini of chaperones heat shock (Hsp)90 and/or Hsp70, and exchange such binding partners is for response. We have previously described design a binds tightly specifically to C-terminus Hsp90, doing so, able inhibit chaperone function vivo. Here we present X-ray crystal structure designed domain (CTPR390) complex with its peptide ligand--the C-terminal residues...
In bacteria, translation of all the ribosomal protein cistrons in spc operon mRNA is repressed by binding product one them, S8, to an internal sequence at 5′ end L5 cistron. The way which first two genes are regulated, retroregulation, mechanistically distinct from translational repression S8 onward. A 2.8 Å resolution crystal structure has been obtained Escherichia coli bound this site. Despite differences, complex almost identical that S8/helix 21 seen small subunit, consistent with...
Abstract The use of MAb E‐9 raised against tissue‐cultured endothelial cells (EC) has shown marked heterogeneity in vascular EC lining the blood vessels normal and tumour tissues. is human EC‐specific protein recognized by it a homodimer with molecular mass 97 kDa. resistant to treatment 3 mM sodium periodate, but sensitive 10% trichloroacetic acid 70% ethanol. been assigned new cluster, CD 105, mapped chromosome 9q3. It approximately homology type‐III cell‐surface receptor for transforming...
Amorphous carbon (a-C) films were fabricated by chemical vapor deposition on SiO2 substrate. The a-C have nano-crystalline sp2 structure with the grain size of ∼5 nm and an optical band gap ∼1.8 eV. show negative magnetoresistance (MR) from 300 to 2 K anomalous shape change MR-magnetic field curves at 10 K. Grain boundary scattering theory weak localization used explain MR mechanism curves.
The bacterial HslVU ATP-dependent protease is a homolog of the eukaryotic 26 S proteasome. HslU ATPase forms hexameric ring, and HslV peptidase dodecamer consisting two stacked rings. In complex, central pores are aligned, proteolytic active sites sequestered in an internal chamber HslV, with access to this restricted small axial pores. Here we show that C-terminal tails play critical role interaction activation peptidase. A synthetic tail peptide 10 amino acids could replace supporting...
Large ATP-dependent proteolytic complexes carry out the majority of intracellular proteolysis. To begin to understand function these proteases at a structural level, we have combined information from number biophysical techniques such as electron microscopy (EM), small-angle scattering, and x-ray crystallography. In this study, exploited inherent symmetry ofEscherichia coliClpP, component ClpAP/XP protease, determine its crystal structure 2.3-Å resolution starting with phase set derived...