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P68 Holin Family
The ''Staphylococcus'' phage P68 Putative Holin (P68 Hol) FamilyTC# 1.E.38 consists of a single putative holinTC# 1.E.38.1.1 from ''Staphylococcus aureus'' phage P68 that is 92 amino acyl residues (aas) in length and exhibits 2 transmembrane segments (TMSs). While annotated as a holin, this protein has not been functionally characterized. /sup> See also * Holin * Lysin * Transporter Classification Database Further reading * Reddy, Bhaskara L.; Saier Jr., Milton H. (2013-11-01)"Topological and phylogenetic analyses of bacterial holin families and superfamilies" ''Biochimica et Biophysica Acta (BBA) - Biomembranes'' 1828 (11): 2654–2671. doi: 10.1016/j.bbamem.2013.07.004. PMC&nbs3788059PMID&nbs23856191 * Saier, Milton H.; Reddy, Bhaskara L. (2015-01-01)"Holins in Bacteria, Eukaryotes, and Archaea: Multifunctional Xenologues with Potential Biotechnological and Biomedical Applications" ''Journal of Bacteriology'' 197(1): 7–17. doi: 10.1128/JB.02046-14. ISSN&nbs0021-9193 PMC& ...
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T1 Holin Family
The Phage T1 Holin (T1 Holin) FamilyTC# 1.E.37 is represented in enterobacterial phages T1, RTP and F20, ''Klebsiella'' phage KP36, and ''Escherichia'' phage ADB-2. All of these possess a putative holin that share a high level of identity. Additionally, Gp9 of ''E. coli'' phage phiE49 is similar in sequence. These proteins are short, 55 to 71 amino acyl residues (aas) in length, and exhibit a single transmembrane segment (TMS). A representative list of proteins belonging to the T1 Holin family can be found in thTransporter Classification Database See also * Holin * Lysin * Transporter Classification Database The Transporter Classification Database (or TCDB) is an International Union of Biochemistry and Molecular Biology (IUBMB)-approved classification system for membrane transport proteins, including ion channels. Classification The upper level of cla ... Further reading * . * . * . * . References {{CCBYSASource, sourcepath=http://tcdb.org/search/result.php?tc=1.E.37, ...
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Holin
Holins are a diverse group of small proteins produced by dsDNA bacteriophages in order to trigger and control the degradation of the host's cell wall at the end of the lytic cycle. Holins form pores in the host's cell membrane, allowing lysins to reach and degrade peptidoglycan, a component of bacterial cell walls. Holins have been shown to regulate the timing of lysis with great precision. Over 50 unrelated gene families encode holins, making them the most diverse group of proteins with common function. Together with lysins, holins are being studied for their potential use as antibacterial agents. While canonical holins act by forming large pores, pinholins such as the S protein of lambdoid phage 21 act by forming heptameric channels that depolarize the bacterial membrane. They are associated with SAR endolysins, which remain inactive in the periplasm prior to the depolarization of the membrane. Viruses that infect eukaryotic cells may use similar channel-forming proteins calle ...
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Lysin
Lysins, also known as endolysins or murein hydrolases, are hydrolase, hydrolytic enzymes produced by bacteriophages in order to cleave the host's cell wall during the final stage of the lytic cycle. Lysins are highly evolved enzymes that are able to target one of the five bonds in peptidoglycan (murein), the main component of bacterial cell walls, which allows the release of progeny virions from the lysed cell. Cell-wall-containing Archaea are also lysed by specialized pseudomurein-cleaving lysins, while most archaeal viruses employ alternative mechanisms. Similarly, not all bacteriophages synthesize lysins: some small single-stranded DNA and RNA phages produce membrane proteins that activate the host's Autolysis (biology), autolytic mechanisms such as autolysins. Lysins were first used therapeutically in 2001 by the Fischetti lab (see below) and are now being used as antibacterial agents due to their high effectiveness and specificity in comparison with antibiotics, which are sus ...
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Transporter Classification Database
The Transporter Classification Database (or TCDB) is an International Union of Biochemistry and Molecular Biology (IUBMB)-approved classification system for membrane transport proteins, including ion channels. Classification The upper level of classification and a few examples of proteins with known 3D structure: 1. Channels and pores 1.A α-type channels * 1.A.1 Voltage-gated ion channel superfamily * 1.A.2 Inward-rectifier K+ channel family * 1.A.3 Ryanodine-inositol-1,4,5-trisphosphate receptor Ca2+ channel family * 1.A.4 Transient receptor potential Ca2+ channel family * 1.A.5 Polycystin cation channel family * 1.A.6 Epithelial Na+ channel family * 1.A.7 ATP-gated P2X receptor cation channel family * 1.A.8 Major intrinsic protein superfamily * 1.A.9 Neurotransmitter receptor, Cys loop, ligand-gated ion channel family * 1.A.10 Glutamate-gated ion channel family of neurotransmitter receptors * 1.A.11 Ammonium channel transporter family * 1.A.12 Intracellular chlorid ...
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Digital Object Identifier
A digital object identifier (DOI) is a persistent identifier or handle used to uniquely identify various objects, standardized by the International Organization for Standardization (ISO). DOIs are an implementation of the Handle System; they also fit within the URI system ( Uniform Resource Identifier). They are widely used to identify academic, professional, and government information, such as journal articles, research reports, data sets, and official publications. A DOI aims to resolve to its target, the information object to which the DOI refers. This is achieved by binding the DOI to metadata about the object, such as a URL where the object is located. Thus, by being actionable and interoperable, a DOI differs from ISBNs or ISRCs which are identifiers only. The DOI system uses the indecs Content Model to represent metadata. The DOI for a document remains fixed over the lifetime of the document, whereas its location and other metadata may change. Referring to ...
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PubMed Central
PubMed Central (PMC) is a free digital repository that archives open access full-text scholarly articles that have been published in biomedical and life sciences journals. As one of the major research databases developed by the National Center for Biotechnology Information (NCBI), PubMed Central is more than a document repository. Submissions to PMC are indexed and formatted for enhanced metadata, medical ontology, and unique identifiers which enrich the XML structured data for each article. Content within PMC can be linked to other NCBI databases and accessed via Entrez search and retrieval systems, further enhancing the public's ability to discover, read and build upon its biomedical knowledge. PubMed Central is distinct from PubMed. PubMed Central is a free digital archive of full articles, accessible to anyone from anywhere via a web browser (with varying provisions for reuse). Conversely, although PubMed is a searchable database of biomedical citations and abstracts, the ...
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PubMed Identifier
PubMed is an openly accessible, free database which includes primarily the MEDLINE database of references and abstracts on life sciences and biomedical topics. The United States National Library of Medicine (NLM) at the National Institutes of Health maintains the database as part of the Entrez system of information retrieval. From 1971 to 1997, online access to the MEDLINE database was provided via computer and phone lines primarily through institutional facilities, such as university libraries. PubMed, first released in January 1996, ushered in the era of private, free, home- and office-based MEDLINE searching. The PubMed system was offered free to the public starting in June 1997. Content In addition to MEDLINE, PubMed provides access to: * older references from the print version of ''Index Medicus'', back to 1951 and earlier * references to some journals before they were indexed in Index Medicus and MEDLINE, for instance ''Science'', '' BMJ'', and ''Annals of Surgery'' ...
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International Standard Serial Number
An International Standard Serial Number (ISSN) is an eight-digit to uniquely identify a periodical publication (periodical), such as a magazine. The ISSN is especially helpful in distinguishing between serials with the same title. ISSNs are used in ordering, cataloging, interlibrary loans, and other practices in connection with serial literature. The ISSN system was first drafted as an International Organization for Standardization (ISO) international standard in 1971 and published as ISO 3297 in 1975. ISO subcommittee TC 46/SC 9 is responsible for maintaining the standard. When a serial with the same content is published in more than one media type, a different ISSN is assigned to each media type. For example, many serials are published both in print and electronic media. The ISSN system refers to these types as print ISSN (p-ISSN) and electronic ISSN (e-ISSN). Consequently, as defined in ISO 3297:2007, every serial in the ISSN system is also assigned a linking ISSN ...
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Protein Families
A protein family is a group of evolutionarily related proteins. In many cases, a protein family has a corresponding gene family, in which each gene encodes a corresponding protein with a 1:1 relationship. The term "protein family" should not be confused with family as it is used in taxonomy. Proteins in a family descend from a common ancestor and typically have similar three-dimensional structures, functions, and significant sequence similarity. Sequence similarity (usually amino-acid sequence) is one of the most common indicators of homology, or common evolutionary ancestry. Some frameworks for evaluating the significance of similarity between sequences use sequence alignment methods. Proteins that do not share a common ancestor are unlikely to show statistically significant sequence similarity, making sequence alignment a powerful tool for identifying the members of protein families. Families are sometimes grouped together into larger clades called superfamilies based on stru ...
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Membrane Proteins
Membrane proteins are common proteins that are part of, or interact with, biological membranes. Membrane proteins fall into several broad categories depending on their location. Integral membrane proteins are a permanent part of a cell membrane and can either penetrate the membrane (Transmembrane protein, transmembrane) or associate with one or the other side of a membrane (Integral monotopic protein, integral monotopic). Peripheral membrane proteins are transiently associated with the cell membrane. Membrane proteins are common, and medically important—about a third of all human proteins are membrane proteins, and these are targets for more than half of all drugs. Nonetheless, compared to other classes of proteins, determining membrane protein structures remains a challenge in large part due to the difficulty in establishing experimental conditions that can preserve the correct (Native state, native) Protein structure, conformation of the protein in isolation from its native ...
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Transmembrane Proteins
A transmembrane protein is a type of integral membrane protein that spans the entirety of the cell membrane. Many transmembrane proteins function as gateways to permit the transport of specific substances across the membrane. They frequently undergo significant conformational changes to move a substance through the membrane. They are usually highly hydrophobic and aggregate and precipitate in water. They require detergents or nonpolar solvents for extraction, although some of them ( beta-barrels) can be also extracted using denaturing agents. The peptide sequence that spans the membrane, or the transmembrane segment, is largely hydrophobic and can be visualized using the hydropathy plot. Depending on the number of transmembrane segments, transmembrane proteins can be classified as single-pass membrane proteins, or as multipass membrane proteins. Some other integral membrane proteins are called monotopic, meaning that they are also permanently attached to the membrane, bu ...
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Transmembrane Transporters
A transmembrane protein is a type of integral membrane protein that spans the entirety of the cell membrane. Many transmembrane proteins function as gateways to permit the transport of specific substances across the membrane. They frequently undergo significant conformational changes to move a substance through the membrane. They are usually highly hydrophobic and aggregate and precipitate in water. They require detergents or nonpolar solvents for extraction, although some of them (beta-barrels) can be also extracted using denaturing agents. The peptide sequence that spans the membrane, or the transmembrane segment, is largely hydrophobic and can be visualized using the hydropathy plot. Depending on the number of transmembrane segments, transmembrane proteins can be classified as single-pass membrane proteins, or as multipass membrane proteins. Some other integral membrane proteins are called monotopic, meaning that they are also permanently attached to the membrane, but do ...
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