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Phage P22 Tailspike Protein
The tailspike protein (P22TSP) of Enterobacteria phage P22 mediates the recognition and adhesion between the bacteriophage and the surface of ''Salmonella enterica'' cells. It is anchored within the viral coat and recognizes the O-antigen portion of the lipopolysaccharide (LPS) on the outer-membrane of Gram-negative bacteria. It possesses endoglycanase activity, serving to shorten the length of the O-antigen during infection. History The initial interest in tailspike proteins was in the study of the effect the mutations on protein folding. Some mutations affect the folding efficiency of the protein but have no effect on the final native structure. Other mutations have been identified that lead to a temperature sensitive phenotype. Reconstitution experiments have demonstrated that the in vitro folding process closely mirrors the in vivo folding pathway. It has been further been demonstrated that folding yields in vitro decrease strongly with increasing temperature. Function ...
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Protein Data Bank
The Protein Data Bank (PDB) is a database for the three-dimensional structural data of large biological molecules, such as proteins and nucleic acids. The data, typically obtained by X-ray crystallography, NMR spectroscopy, or, increasingly, cryo-electron microscopy, and submitted by biologists and biochemists from around the world, are freely accessible on the Internet via the websites of its member organisations (PDBe, PDBj, RCSB, and BMRB). The PDB is overseen by an organization called the Worldwide Protein Data Bank, wwPDB. The PDB is a key in areas of structural biology, such as structural genomics. Most major scientific journals and some funding agencies now require scientists to submit their structure data to the PDB. Many other databases use protein structures deposited in the PDB. For example, SCOP and CATH classify protein structures, while PDBsum provides a graphic overview of PDB entries using information from other sources, such as Gene ontology. History Two force ...
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Endoglycosidase
An Endoglycosidase is an enzyme that releases oligosaccharides from glycoproteins or glycolipids. It may also cleave polysaccharide chains between residues that are not the terminal residue, although releasing oligosaccharides from conjugated protein and lipid molecules is more common. It breaks the glycosidic bonds between two sugar monomer in the polymer. It is different from exoglycosidase that it does not do so at the terminal residue. Hence, it is used to release long carbohydrates from conjugated molecules. If an exoglycosidase were used, every monomer in the polymer would have to be removed, one by one from the chain, taking a long time. An endoglycosidase cleaves, giving a polymeric product. PROTEIN-x1-x2-x3-x4-x5-x6-x7-x8-x9-x10-x11-...-xn Mechanism Overview The mechanism is an enzymatic hydrolysis that requires two critical molecules; a proton donor (most likely an acid) and a nucleophile(most likely a base). The Endoglycosidases mechanism has two forms; an acid catalyz ...
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Protein Domain
In molecular biology, a protein domain is a region of a protein's polypeptide chain that is self-stabilizing and that folds independently from the rest. Each domain forms a compact folded three-dimensional structure. Many proteins consist of several domains, and a domain may appear in a variety of different proteins. Molecular evolution uses domains as building blocks and these may be recombined in different arrangements to create proteins with different functions. In general, domains vary in length from between about 50 amino acids up to 250 amino acids in length. The shortest domains, such as zinc fingers, are stabilized by metal ions or disulfide bridges. Domains often form functional units, such as the calcium-binding EF hand domain of calmodulin. Because they are independently stable, domains can be "swapped" by genetic engineering between one protein and another to make chimeric proteins. Background The concept of the domain was first proposed in 1973 by Wetlaufer aft ...
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Solenoid Protein Domain
Solenoid protein domains are a highly modular type of protein domain. They consist of a chain of nearly identical folds, often simply called tandem repeats. They are extremely common among all types of proteins, though exact figures are unknown. "Repeats" in molecular biology In proteins, a "repeat" is any sequence block that returns more than one time in the sequence, either in an identical or a highly similar form. Repetitiveness does not in itself indicate anything about the structure of the protein. As a "rule of thumb", short repetitive sequences (e.g. those below the length of 10 amino acids) may be intrinsically disordered, and not part of any folded protein domains. Repeats that are at least 30 to 40 amino acids long, are far more likely to be folded as part of a domain. Such long repeats are frequently indicative of the presence of a solenoid domain in the protein. Examples of disordered repetitive sequences include the 7-mer peptide repeats found in the RPB1 subun ...
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Beta Helix
A beta helix is a tandem protein repeat structure formed by the association of parallel beta strands in a helical pattern with either two or three faces. The beta helix is a type of solenoid protein domain. The structure is stabilized by inter-strand hydrogen bonds, protein-protein interactions, and sometimes bound metal ions. Both left- and right-handed beta helices have been identified. These structures are distinct from jelly-roll folds, a different protein structure sometimes known as a "double-stranded beta helix". The first beta-helix was observed in the enzyme pectate lyase, which contains a seven-turn helix that reaches 34 Å (3.4 nm) long. The P22 phage tail spike protein, a component of the P22 bacteriophage, has 13 turns and in its assembled homo trimer is 200 Å (20 nm) in length. Its interior is close-packed with no central pore and contains both hydrophobic residues and charged residues neutralized by salt bridges. Both pectate lyase and P22 tailspike prote ...
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Monomer
In chemistry, a monomer ( ; ''mono-'', "one" + '' -mer'', "part") is a molecule that can react together with other monomer molecules to form a larger polymer chain or three-dimensional network in a process called polymerization. Classification Monomers can be classified in many ways. They can be subdivided into two broad classes, depending on the kind of the polymer that they form. Monomers that participate in condensation polymerization have a different stoichiometry than monomers that participate in addition polymerization: : Other classifications include: *natural vs synthetic monomers, e.g. glycine vs caprolactam, respectively *polar vs nonpolar monomers, e.g. vinyl acetate vs ethylene, respectively *cyclic vs linear, e.g. ethylene oxide vs ethylene glycol, respectively The polymerization of one kind of monomer gives a homopolymer. Many polymers are copolymers, meaning that they are derived from two different monomers. In the case of condensation polymerizations, the r ...
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Space Group
In mathematics, physics and chemistry, a space group is the symmetry group of an object in space, usually in three dimensions. The elements of a space group (its symmetry operations) are the rigid transformations of an object that leave it unchanged. In three dimensions, space groups are classified into 219 distinct types, or 230 types if chiral copies are considered distinct. Space groups are discrete cocompact groups of isometries of an oriented Euclidean space in any number of dimensions. In dimensions other than 3, they are sometimes called Bieberbach groups. In crystallography, space groups are also called the crystallographic or Fedorov groups, and represent a description of the symmetry of the crystal. A definitive source regarding 3-dimensional space groups is the ''International Tables for Crystallography'' . History Space groups in 2 dimensions are the 17 wallpaper groups which have been known for several centuries, though the proof that the list was complete was only ...
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Capsid
A capsid is the protein shell of a virus, enclosing its genetic material. It consists of several oligomeric (repeating) structural subunits made of protein called protomers. The observable 3-dimensional morphological subunits, which may or may not correspond to individual proteins, are called capsomeres. The proteins making up the capsid are called capsid proteins or viral coat proteins (VCP). The capsid and inner genome is called the nucleocapsid. Capsids are broadly classified according to their structure. The majority of the viruses have capsids with either helical or icosahedral structure. Some viruses, such as bacteriophages, have developed more complicated structures due to constraints of elasticity and electrostatics. The icosahedral shape, which has 20 equilateral triangular faces, approximates a sphere, while the helical shape resembles the shape of a spring, taking the space of a cylinder but not being a cylinder itself. The capsid faces may consist of one or more ...
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Amino Acid
Amino acids are organic compounds that contain both amino and carboxylic acid functional groups. Although hundreds of amino acids exist in nature, by far the most important are the alpha-amino acids, which comprise proteins. Only 22 alpha amino acids appear in the genetic code. Amino acids can be classified according to the locations of the core structural functional groups, as Alpha and beta carbon, alpha- , beta- , gamma- or delta- amino acids; other categories relate to Chemical polarity, polarity, ionization, and side chain group type (aliphatic, Open-chain compound, acyclic, aromatic, containing hydroxyl or sulfur, etc.). In the form of proteins, amino acid '' residues'' form the second-largest component (water being the largest) of human muscles and other tissues. Beyond their role as residues in proteins, amino acids participate in a number of processes such as neurotransmitter transport and biosynthesis. It is thought that they played a key role in enabling life ...
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Infection
An infection is the invasion of tissues by pathogens, their multiplication, and the reaction of host tissues to the infectious agent and the toxins they produce. An infectious disease, also known as a transmissible disease or communicable disease, is an illness resulting from an infection. Infections can be caused by a wide range of pathogens, most prominently bacteria and viruses. Hosts can fight infections using their immune system. Mammalian hosts react to infections with an innate response, often involving inflammation, followed by an adaptive response. Specific medications used to treat infections include antibiotics, antivirals, antifungals, antiprotozoals, and antihelminthics. Infectious diseases resulted in 9.2 million deaths in 2013 (about 17% of all deaths). The branch of medicine that focuses on infections is referred to as infectious disease. Types Infections are caused by infectious agents (pathogens) including: * Bacteria (e.g. ''Mycobacterium tuberculosis'', ...
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Membrane
A membrane is a selective barrier; it allows some things to pass through but stops others. Such things may be molecules, ions, or other small particles. Membranes can be generally classified into synthetic membranes and biological membranes. Biological membranes include cell membranes (outer coverings of cells or organelles that allow passage of certain constituents); nuclear membranes, which cover a cell nucleus; and tissue membranes, such as mucosae and serosae. Synthetic membranes are made by humans for use in laboratories and industry (such as chemical plants). This concept of a membrane has been known since the eighteenth century but was used little outside of the laboratory until the end of World War II. Drinking water supplies in Europe had been compromised by the war and membrane filters were used to test for water safety. However, due to the lack of reliability, slow operation, reduced selectivity and elevated costs, membranes were not widely exploited. The first us ...
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Enzyme
Enzymes () are proteins that act as biological catalysts by accelerating chemical reactions. The molecules upon which enzymes may act are called substrates, and the enzyme converts the substrates into different molecules known as products. Almost all metabolic processes in the cell need enzyme catalysis in order to occur at rates fast enough to sustain life. Metabolic pathways depend upon enzymes to catalyze individual steps. The study of enzymes is called ''enzymology'' and the field of pseudoenzyme analysis recognizes that during evolution, some enzymes have lost the ability to carry out biological catalysis, which is often reflected in their amino acid sequences and unusual 'pseudocatalytic' properties. Enzymes are known to catalyze more than 5,000 biochemical reaction types. Other biocatalysts are catalytic RNA molecules, called ribozymes. Enzymes' specificity comes from their unique three-dimensional structures. Like all catalysts, enzymes increase the reaction ra ...
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