scholarly journals Stringent Primer Termination by an Archaeo-Eukaryotic DNA Primase

2021 ◽  
Vol 12 ◽  
Author(s):  
Jan Bergsch ◽  
Jean-Christophe Devillier ◽  
Gunnar Jeschke ◽  
Georg Lipps
Keyword(s):  
Catalytic Domain ◽  
Unit Length ◽  
Structural Features ◽  
Fundamental Function ◽  
Dna Primase ◽  
Sulfolobus Islandicus ◽  
Mechanistic Investigation ◽  
Eukaryotic Dna ◽  
Apparent Ability ◽  
Made In

Priming of single stranded templates is essential for DNA replication. In recent years, significant progress was made in understanding how DNA primase fulfils this fundamental function, particularly with regard to the initiation. Equally intriguing is the unique property of archeao-eukaryotic primases to terminate primer formation at a well-defined unit length. The apparent ability to “count” the number of bases incorporated prior to primer release is not well understood, different mechanisms having been proposed for different species. We report a mechanistic investigation of primer termination by the pRN1 primase from Sulfolobus islandicus. Using an HPLC-based assay we determined structural features of the primer 5′-end that are required for consistent termination. Mutations within the unstructured linker connecting the catalytic domain to the template binding domain allowed us to assess the effect of altered linker length and flexibility on primer termination.

Algorithms structural and parametric synthesis of remote control and diagnostics systems of mobile measuring points

2018 ◽  
pp. 60-65
Author(s):  
A. I. Tatarinov
Keyword(s):  
Complex System ◽  
Control System ◽  
Remote Control ◽  
Structural Features ◽  
Information Protection ◽  
Parametric Synthesis ◽  
Unauthorized Access ◽  
Operating Modes ◽  
Remote Control System ◽  
Made In

With the help of the general and structurally-information schemes of remote control, an analysis was made in the course of which the requirements for protection against unauthorized access of the complex system were clarified and established. In the article structural features of the remote control system of mobile measuring points of rocket and space equipment are considered. These features are represented by the requirements for information protection, as well as the operating modes of this system. The list of these regimes was obtained as a result of studies of structural and functional schemes of a remote control system for mobile measuring points.

Developments in Rechargeable Mno2Electrodes for Lithium Batteries

1988 ◽  
Vol 135 ◽  
Author(s):  
Michael M Thackeray
Keyword(s):  
Lithium Batteries ◽  
Lithium Battery ◽  
Electrode Materials ◽  
State Of The Art ◽  
Structural Features ◽  
Rechargeable Batteries ◽  
Current State ◽  
Alternative Systems ◽  
Battery Technology ◽  
Made In

AbstractConsiderable efforts are in progress to develop rechargeable batteries as alternative systems to the nickel-cadmium battery. In this regard, several advances have been made in ambient-temperature lithium battery technology, and specifically in the engineering of rechargeable lithium/manganese dioxide cells. This paper reviews the current state of the art in rechargeable Li/MnO2battery technology; particular attention is paid to the structural features of various MnO2electrode materials which influence their electrochemical and cycling behaviour in lithium cells.

Structural insights into dihydroxylation of terephthalate, a product of polyethylene terephthalate degradation

2022 ◽  
Author(s):  
Jai Krishna Mahto ◽  
Neetu Neetu ◽  
Monica Sharma ◽  
Monika Dubey ◽  
Bhanu Prakash Vellanki ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Substrate Specificity ◽  
Polyethylene Terephthalate ◽  
Active Site ◽  
Catalytic Domain ◽  
Structural Features ◽  
Comamonas Testosteroni ◽  
Plastic Pollution ◽  
Microbial Utilization ◽  
Steady State Kinetics

Biodegradation of terephthalate (TPA) is a highly desired catabolic process for the bacterial utilization of this Polyethylene terephthalate (PET) depolymerization product, but to date, the structure of terephthalate dioxygenase (TPDO), a Rieske oxygenase (RO) that catalyzes the dihydroxylation of TPA to a cis -diol is unavailable. In this study, we characterized the steady-state kinetics and first crystal structure of TPDO from Comamonas testosteroni KF1 (TPDO KF1 ). The TPDO KF1 exhibited the substrate specificity for TPA ( k cat / K m = 57 ± 9 mM −1 s −1 ). The TPDO KF1 structure harbors characteristics RO features as well as a unique catalytic domain that rationalizes the enzyme’s function. The docking and mutagenesis studies reveal that its substrate specificity to TPA is mediated by Arg309 and Arg390 residues, two residues positioned on opposite faces of the active site. Additionally, residue Gln300 is also proven to be crucial for the activity, its substitution to alanine decreases the activity ( k cat ) by 80%. Together, this study delineates the structural features that dictate the substrate recognition and specificity of TPDO. Importance The global plastic pollution has become the most pressing environmental issue. Recent studies on enzymes depolymerizing polyethylene terephthalate plastic into terephthalate (TPA) show some potential in tackling this. Microbial utilization of this released product, TPA is an emerging and promising strategy for waste-to-value creation. Research from the last decade has discovered terephthalate dioxygenase (TPDO), as being responsible for initiating the enzymatic degradation of TPA in a few Gram-negative and Gram-positive bacteria. Here, we have determined the crystal structure of TPDO from Comamonas testosteroni KF1 and revealed that it possesses a unique catalytic domain featuring two basic residues in the active site to recognize TPA. Biochemical and mutagenesis studies demonstrated the crucial residues responsible for the substrate specificity of this enzyme.

scholarly journals Structure and function of factor XI

Blood ◽  
2010 ◽  
Vol 115 (13) ◽  
pp. 2569-2577 ◽  
Author(s):  
Jonas Emsley ◽  
Paul A. McEwan ◽  
David Gailani
Keyword(s):  
Catalytic Domain ◽  
Structural Features ◽  
Factor Ix ◽  
Missense Mutations ◽  
Factor Xi ◽  
Disk Structure ◽  
Ligand Binding Sites ◽  
And Function ◽  
Insight Into

AbstractFactor XI (FXI) is the zymogen of an enzyme (FXIa) that contributes to hemostasis by activating factor IX. Although bleeding associated with FXI deficiency is relatively mild, there has been resurgence of interest in FXI because of studies indicating it makes contributions to thrombosis and other processes associated with dysregulated coagulation. FXI is an unusual dimeric protease, with structural features that distinguish it from vitamin K–dependent coagulation proteases. The recent availability of crystal structures for zymogen FXI and the FXIa catalytic domain have enhanced our understanding of structure-function relationships for this molecule. FXI contains 4 “apple domains” that form a disk structure with extensive interfaces at the base of the catalytic domain. The characterization of the apple disk structure, and its relationship to the catalytic domain, have provided new insight into the mechanism of FXI activation, the interaction of FXIa with the substrate factor IX, and the binding of FXI to platelets. Analyses of missense mutations associated with FXI deficiency have provided additional clues to localization of ligand-binding sites on the protein surface. Together, these data will facilitate efforts to understand the physiology and pathology of this unusual protease, and development of therapeutics to treat thrombotic disorders.

scholarly journals Eukaryotic DNA primase appears to act as oligomer in DNA-polymerase-alpha-primase complex

1992 ◽  
Vol 206 (1) ◽  
pp. 7-13 ◽  
Author(s):  
Vladimir N. PODUST ◽  
Olga V. VLADIMIROVA ◽  
Elena N. MANAKOVA ◽  
Olga I. LAVRIK
Keyword(s):  
Dna Polymerase ◽  
Dna Polymerase Alpha ◽  
Dna Primase ◽  
Eukaryotic Dna ◽  
Primase Complex

scholarly journals A trapped human PPM1A–phosphopeptide complex reveals structural features critical for regulation of PPM protein phosphatase activity

2018 ◽  
Vol 293 (21) ◽  
pp. 7993-8008 ◽  
Author(s):  
Subrata Debnath ◽  
Dalibor Kosek ◽  
Harichandra D. Tagad ◽  
Stewart R. Durell ◽  
Daniel H. Appella ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Metal Ions ◽  
Active Site ◽  
Metal Binding ◽  
Metal Ion ◽  
Catalytic Domain ◽  
Protein Phosphatases ◽  
Random Order ◽  
Structural Features

Metal-dependent protein phosphatases (PPM) are evolutionarily unrelated to other serine/threonine protein phosphatases and are characterized by their requirement for supplementation with millimolar concentrations of Mg2+ or Mn2+ ions for activity in vitro. The crystal structure of human PPM1A (also known as PP2Cα), the first PPM structure determined, displays two tightly bound Mn2+ ions in the active site and a small subdomain, termed the Flap, located adjacent to the active site. Some recent crystal structures of bacterial or plant PPM phosphatases have disclosed two tightly bound metal ions and an additional third metal ion in the active site. Here, the crystal structure of the catalytic domain of human PPM1A, PPM1Acat, complexed with a cyclic phosphopeptide, c(MpSIpYVA), a cyclized variant of the activation loop of p38 MAPK (a physiological substrate of PPM1A), revealed three metal ions in the active site. The PPM1Acat D146E–c(MpSIpYVA) complex confirmed the presence of the anticipated third metal ion in the active site of metazoan PPM phosphatases. Biophysical and computational methods suggested that complex formation results in a slightly more compact solution conformation through reduced conformational flexibility of the Flap subdomain. We also observed that the position of the substrate in the active site allows solvent access to the labile third metal-binding site. Enzyme kinetics of PPM1Acat toward a phosphopeptide substrate supported a random-order, bi-substrate mechanism, with substantial interaction between the bound substrate and the labile metal ion. This work illuminates the structural and thermodynamic basis of an innate mechanism regulating the activity of PPM phosphatases.

Corrosion of Si3N4-Ceramics in Acids and Basics

2006 ◽  
Vol 45 ◽  
pp. 148-155 ◽  
Author(s):  
Jochen Schilm ◽  
Mathias Herrmann ◽  
G. Michael
Keyword(s):  
Silicon Nitride ◽  
Grain Boundary ◽  
Corrosion Behavior ◽  
Aqueous Media ◽  
Structural Features ◽  
Boundary Phase ◽  
The Subject ◽  
Corrosion Mechanisms ◽  
Si3n4 Ceramics ◽  
Made In

The corrosion behavior of silicon nitride materials in aqueous media strongly depends on the composition and amount of the grain boundary. But there exist no systematic investigations of the relation between the corrosion behavior and the composition and amount of the grain-boundary phase. The subject of this study is based on the evaluation of the corrosion mechanisms of Si3N4 ceramics and YSiAlON glasses, both with defined and characterized compositions, in acidic and basic environments with different concentrations. Special effort has been made in describing the compositions of grain boundary phases in the sintered Si3N4 ceramics. A model to describe structural features of YSiAlON-glasses was developed which allows the correlation of the corrosion behavior of the ceramics and the glasses with their compositions. In combination with SEM and TEM investigations it became possible to give structural reasons for the different observed corrosion mechanisms.

The Interaction of Synthetic Templates with Eukaryotic DNA Primase

1995 ◽  
Vol 228 (1) ◽  
pp. 60-67 ◽  
Author(s):  
Rashid O. Anarbaev ◽  
Olga V. Vladimirova ◽  
Olga I. Lavrik
Keyword(s):  
Dna Primase ◽  
Eukaryotic Dna

Structural features and nucleotide-binding capability of the C subunit are integral to the regulation of the eukaryotic V1Vo ATPases

2005 ◽  
Vol 33 (4) ◽  
pp. 883-885 ◽  
Author(s):  
G. Grüber
Keyword(s):  
Conformational Changes ◽  
Atp Hydrolysis ◽  
Structural Features ◽  
Subunit C ◽  
Reversible Dissociation ◽  
Intracellular Compartments ◽  
C Subunit ◽  
Vacuolar Atpases ◽  
Made In

V-ATPases (vacuolar ATPases) are responsible for acidification of intracellular compartments and, in certain cases, proton transport across the plasma membrane of eukaryotic cells. They are composed of a catalytic V1 sector, in which ATP hydrolysis takes place, and the Vo sector, which functions in proton conduction. The best established mechanism for regulating the V-ATPase activity in vivo involves reversible dissociation of the V1 and Vo domains, in which subunit C is intimately involved. In the last year, impressive progress has been made in elucidating the structure of the C subunit and its arrangement inside the V-ATPase. Nucleotide occupancy by subunit C, followed by conformational changes of this subunit has shed light on the mechanism of V-ATPase regulation.

scholarly journals Structural and Functional Characteristics of ADAMTS-4 and ADAMTS-5: A Review

2020 ◽  
pp. 12-21
Author(s):  
Anastasia Korchagina ◽  
Lyudmila Derevshchikova
Keyword(s):  
Enzymatic Activity ◽  
Binding Sites ◽  
Catalytic Domain ◽  
Structural Features ◽  
Functional Characteristics ◽  
Rich Domain ◽  
Common Diseases ◽  
The Moment ◽  
Cysteine Rich Domain

ADAMTS-4 and -5 are aggrecanases that are involved in the development of osteoarthrosis, one of the most common diseases at the moment, due to which a large number of people suffer annually. By some estimates, 9.6% of men and 18% of women over the age of 60 have symptomatic osteoarthrosis. This review discusses the currently known data on the structural features and enzymatic activity of these enzymes. The structures of ADAMTS-4 and -5 are similar, they contain 7 domain sites: the signal section, the N-terminal prodomain, the catalytic domain, the disintegrin-like domain, the thrombospodin motif, the cysteine-rich domain, and the spacer domain. In addition to all these elements, ADAMTS-5 has an additional thrombospodin motif at the end. ADAMTS-4 and -5 cleaves aggrecan in 5 different binding sites. However, the Glu373-Ala374 site probably plays the most important role in the pathogenesis, since when this bond is broken, the whole aggrecan molecule loses its integrity, which leads to the destruction of cartilage and the development of the disease. In the course of the analysis of the information, the authors have found that the participation of ADAMTS-4 and -5 in the development of osteoarthritis varies greatly depending on the type of organism. The researchers have established that in mice ADAMTS-4 plays the largest role in the destruction of aggrecan, while in humans ADAMTS-5 or both aggrecanases influence the development of osteoarthritis. The revealed differences are not fully described; therefore, this review summarizes the already known results in this area, which will facilitate further research in this direction.

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