Encapsulin Nanocompartment
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Encapsulin Nanocompartment
Encapsulin nanocompartments, or encapsulin protein cages, are spherical bacterial organelle-like compartments roughly 25-30 nm in diameter that are involved in various aspects of metabolism, in particular protecting bacteria from oxidative stress. Encapsulin nanocompartments are structurally similar to the HK97 bacteriophage and their function depends on the proteins loaded into the nanocompartment. The sphere is formed from 60 (for a 25 nm sphere) or 180 (for a 30 nm sphere) copies of a single protomer, termed encapsulin. Their structure has been studied in great detail using X-ray crystallography and cryo-electron microscopy. A number of different types of proteins have been identified as being loaded into encapsulin nanocompartments. Peroxidases or proteins similar to ferritin Ferritin is a universal intracellular protein that stores iron and releases it in a controlled fashion. The protein is produced by almost all living organisms, including archaea, bact ...
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Thermotoga Maritima Encapsulin
''Thermotoga'' is a genus of the phylum '' Thermotogota''. Members of ''Thermotoga'' are hyperthermophilic bacteria whose cell is wrapped in a unique sheath-like outer membrane, called a "toga". The members of the phylum stain Gram-negative as they possess a thin peptidoglycan in between two lipid bilayers, albeit both peculiar. The peptidoglycan is unusual as the crosslink is not only meso-diaminopimelate as occurs in Pseudomonadota, but D-lysine.All proteinogenic amino acids have the L- configuration; in peptidoglycan some amino acids with the D- configuration are present. Lysine is synthesised from meso-diaminopimelate by Diaminopimelate decarboxylase The species are anaerobes with varying degrees of oxygen tolerance. They are capable of reducing elemental sulphur (S0) to hydrogen sulphide, which in turn can be used. Whether thermophily is an innovation of the lineage or an ancestral trait is unclear and cannot be determined. The genome of '' Thermotoga maritima'' was seque ...
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HK97
''Escherichia virus HK97'', often shortened to HK97, is a species of virus that infects ''Escherichia coli'' and related bacteria. It is named after Hong Kong (HK), where it was first located. HK97 has a double-stranded DNA genome. Assembly and maturation The major capsid protein of HK97, called gp5, cross-links upon maturation to form a chain-mail like structure. While DNA is being packaged into the capsid, the capsid expands by nearly 5 nm and changes from spherical to icosahedral in shape. The HK97 assembly pathway begins with self-assembly of gp5 into pentamers and hexamers. A protease, called gp4, cleaves gp5 at its N-terminus. Attachment of a portal protein, gp3, coupled with conformational changes leads to the formation of a prohead, or procapsid, which is the precursor to the mature capsid. A scaffolding protein In biology, scaffold proteins are crucial regulators of many key signalling pathways. Although scaffolds are not strictly defined in function, they are k ...
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Protomer
In structural biology, a protomer is the structural unit of an oligomeric protein. It is the smallest unit composed of at least two different protein chains that form a larger hetero-oligomer by association of two or more copies of this unit. The term was introduced by Chetverin to make nomenclature in the Na/K-ATPase enzyme unambiguous. This enzyme is composed of two subunits: a large, catalytic α subunit, and a smaller glycoprotein β subunit (plus a proteolipid, called γ-subunit). At the time it was unclear how many of each work together. In addition, when people spoke of a dimer, it was unclear whether they were referring to αβ or to (αβ)2. Chetverin suggested to call αβ a protomer and (αβ)2 a diprotomer. Protomers usually arrange in cyclic symmetry to form closed point group symmetries. In chemistry, a so-called protomer is a molecule which displays tautomerism due to position of a proton. Examples Hemoglobin is a heterotetramer consisting of four subunits (two α ...
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Encapsulin
The encapsulins are a family of bacterial proteins that serve as the main structural components of encapsulin nanocompartments. There are several different encapsulin proteins, including EncA, which forms the shell, and EncB, EncC, and EncD, which form the core. References {{reflist Cell biology Metabolism Biological engineering Bacterial proteins ...
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X-ray Crystallography
X-ray crystallography is the experimental science determining the atomic and molecular structure of a crystal, in which the crystalline structure causes a beam of incident X-rays to diffract into many specific directions. By measuring the angles and intensities of these diffracted beams, a crystallographer can produce a three-dimensional picture of the density of electrons within the crystal. From this electron density, the mean positions of the atoms in the crystal can be determined, as well as their chemical bonds, their crystallographic disorder, and various other information. Since many materials can form crystals—such as salts, metals, minerals, semiconductors, as well as various inorganic, organic, and biological molecules—X-ray crystallography has been fundamental in the development of many scientific fields. In its first decades of use, this method determined the size of atoms, the lengths and types of chemical bonds, and the atomic-scale differences among various mat ...
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Cryo-electron Microscopy
Cryogenic electron microscopy (cryo-EM) is a cryomicroscopy technique applied on samples cooled to cryogenic temperatures. For biological specimens, the structure is preserved by embedding in an environment of vitreous ice. An aqueous sample solution is applied to a grid-mesh and plunge-frozen in liquid ethane or a mixture of liquid ethane and propane. While development of the technique began in the 1970s, recent advances in detector technology and software algorithms have allowed for the determination of biomolecular structures at near-atomic resolution. This has attracted wide attention to the approach as an alternative to X-ray crystallography or NMR spectroscopy for macromolecular structure determination without the need for crystallization. In 2017, the Nobel Prize in Chemistry was awarded to Jacques Dubochet, Joachim Frank, and Richard Henderson "for developing cryo-electron microscopy for the high-resolution structure determination of biomolecules in solution." ''Nature M ...
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Peroxidase
Peroxidases or peroxide reductases ( EC numberbr>1.11.1.x are a large group of enzymes which play a role in various biological processes. They are named after the fact that they commonly break up peroxides. Functionality Peroxidases typically catalyze a reaction of the form: :ROOR' + \overset + 2H+ -> ce + R'OH Optimal substrates For many of these enzymes the optimal substrate is hydrogen peroxide, but others are more active with organic hydroperoxides such as lipid peroxides. Peroxidases can contain a heme cofactor in their active sites, or alternately redox-active cysteine or selenocysteine residues. The nature of the electron donor is very dependent on the structure of the enzyme. * For example, horseradish peroxidase can use a variety of organic compounds as electron donors and acceptors. Horseradish peroxidase has an accessible active site, and many compounds can reach the site of the reaction. * On the other hand, for an enzyme such as cytochrome c peroxidase, the co ...
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Ferritin
Ferritin is a universal intracellular protein that stores iron and releases it in a controlled fashion. The protein is produced by almost all living organisms, including archaea, bacteria, algae, higher plants, and animals. It is the primary ''intracellular iron-storage protein'' in both prokaryotes and eukaryotes, keeping iron in a soluble and non-toxic form. In humans, it acts as a buffer against iron deficiency and iron overload. Ferritin is found in most tissues as a cytosolic protein, but small amounts are secreted into the serum where it functions as an iron carrier. Plasma ferritin is also an indirect marker of the total amount of iron stored in the body; hence, serum ferritin is used as a diagnostic test for iron-deficiency anemia. Aggregated ferritin transforms into a toxic form of iron called hemosiderin. Ferritin is a globular protein complex consisting of 24 protein subunits forming a hollow nanocage with multiple metal–protein interactions. Ferritin that is n ...
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Metabolism
Metabolism (, from el, μεταβολή ''metabolē'', "change") is the set of life-sustaining chemical reactions in organisms. The three main functions of metabolism are: the conversion of the energy in food to energy available to run cellular processes; the conversion of food to building blocks for proteins, lipids, nucleic acids, and some carbohydrates; and the elimination of metabolic wastes. These enzyme-catalyzed reactions allow organisms to grow and reproduce, maintain their structures, and respond to their environments. The word metabolism can also refer to the sum of all chemical reactions that occur in living organisms, including digestion and the transportation of substances into and between different cells, in which case the above described set of reactions within the cells is called intermediary (or intermediate) metabolism. Metabolic reactions may be categorized as ''catabolic'' – the ''breaking down'' of compounds (for example, of glucose to pyruvate by ce ...
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Cell Biology
Cell biology (also cellular biology or cytology) is a branch of biology that studies the structure, function, and behavior of cells. All living organisms are made of cells. A cell is the basic unit of life that is responsible for the living and functioning of organisms. Cell biology is the study of structural and functional units of cells. Cell biology encompasses both prokaryotic and eukaryotic cells and has many subtopics which may include the study of cell metabolism, cell communication, cell cycle, biochemistry, and cell composition. The study of cells is performed using several microscopy techniques, cell culture, and cell fractionation. These have allowed for and are currently being used for discoveries and research pertaining to how cells function, ultimately giving insight into understanding larger organisms. Knowing the components of cells and how cells work is fundamental to all biological sciences while also being essential for research in biomedical fields such as ...
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Biological Engineering
Biological engineering or bioengineering is the application of principles of biology and the tools of engineering to create usable, tangible, economically-viable products. Biological engineering employs knowledge and expertise from a number of pure and applied sciences, such as mass and heat transfer, kinetics, biocatalysts, biomechanics, bioinformatics, separation and purification processes, bioreactor design, surface science, fluid mechanics, thermodynamics, and polymer science. It is used in the design of medical devices, diagnostic equipment, biocompatible materials, renewable energy, ecological engineering, agricultural engineering, process engineering and catalysis, and other areas that improve the living standards of societies. Examples of bioengineering research include bacteria engineered to produce chemicals, new medical imaging technology, portable and rapid disease diagnostic devices, prosthetics, biopharmaceuticals, and tissue-engineered organs. Bioengineering ...
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