- Heptamer
An heptamer is a thing composed out of seven sub unit s. See also wiktionary Heptamer Heptameria , a genus of fungi in the class Dothideomycetes Heptam ron , a collection of 72 short stories written in French by Marguerite of Navarre and published in 1558 Hepta , a prefix mer , an affix chemistry stub Category Oligomers ... more details
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- -mer
Dicdef Multiple issues prose May 2011 unreferenced October 2010 notability May 2011 Other uses Mer disambiguation Mer wiktionarypar mer mer and mer from Greek meros , part are affix es used in the following words. Chemistry or biochemistry Monomer Dimer Trimer Tetramer Pentamer Hexamer Heptamer Octamer Nonamer Decamer Dodecamer Oligomer Polymer Enantiomer Heteromer Homeomer Isomer Biology Merosity , a characteristic regarding the flower petals number in plants Metamery , a characteristic of segmented animals Category suffixes Category prefixes de mer vocab stub chem stub ... more details
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- Recombination signal sequences
Unreferenced date January 2009 The regional genes V, D, J , used to generate T cell receptor T cell receptors and Antibody Immunoglobulin molecules , are flanked by Recombination Signal Sequences RSSs that are recognized by a group of enzymes known collectively as the VDJ recombinase. RSSs are composed of seven conserved nucleotides a heptamer that reside next to the gene encoding sequence followed by a spacer containing either 12 or 23 unconserved nucleotides followed by a conserved nonamer 9 base pairs . The RSSs are present on the Directionality molecular biology 3 side downstream of a V region and the Directionality molecular biology 5 side upstream of the J region. These are the sides that will be involved in the joining. Only a pair of dissimilar spacer RSSs are efficiently genetic recombination recombined i.e. one with a spacer of 12 nucleotides will be recombined with one that has a spacer containing 23 nucleotides . This is known as the 12 23 rule of recombination or the one turn two turn rule . See also VDJ recombination Category Immune system immunology stub ... more details
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- Anthrax toxin
6 Ribbon diagram of a PA sub 63 sub heptamer forming a pre pore. Petosa et al.solved the structure of a PA63 heptamer at 4.5 0.45 nm Fig. 6 . ref name Petosa The structure they solved was of a non membrane bound pre pore, the conformation of the heptamer before the complex extends a barrel ..., the pre pore is quickly formed. The heptamer formation causes no major changes in the conformation ... bind to the heptamer pre pore. This binding occurs because after removing the PA20 domain ... with domain 1 of two adjacent PA63 molecules when in the heptamer conformation. ref Melnyk, R. A. Hewitt ... molecules on a PA63 heptamer. The LF EF binding site is now being utilized for delivery of therapeutics via fusion proteins. Upon formation of the prepore and attachment of LF and or EF, the heptamer ... and before LF or EF can associate with the heptamer. Reassociation of the receptor with the cholesterol ... is transferred to an acidic compartment, where the heptamer, still in the non membrane spanning ... of the PA Greek key motifs into the membrane occurs when the heptamer is acidified. On artificial bilayers ... transition is the initial step of PA membrane insertion. PA is endocytosed as a soluble heptamer attached to its receptors, with LF or EF attached to the heptamer as cargo. The first step after endocytosis ... 2 to fold out of the heptamer pre pore and insert through the wall of the acidic vesicle, leading ... more acidic conditions are met. These histidines all work in conjunction to keep the heptamer from ... more details
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- Mechanosensitive ion channel
terminal helices are conserved. MscS folds as a homo heptamer with a cylindrical shape, and can be divided ... more details
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- Recombination activating gene
heptamer a conserved region of 7 nucleotides that is adjacent to the coding sequence, leaving ... heptamer. The core region of RAG 2 is predicted to form a six bladed beta propeller structure that appears ... more details
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- Water cluster
can be used. In a recent study the conformation of a water heptamer was determined cyclic ... of an Elusive Discrete Cyclic Water Heptamer to a Bicyclic H2O 7 Cluster author M. H. Mir, J ... more details
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- Chaperonin
Chaperonins are proteins that fold and unfold other proteins. Newly made proteins usually must protein folding fold from a linear chain of amino acids into a three dimensional form. Chaperonins belong to a large class of molecules that assist protein folding, called molecular chaperones . ref http www.hhmi.org research investigators horwich bio.html Howard Hughes Investigators Arthur L. Horwich, M.D. ref The energy to fold proteins is supplied by adenosine triphosphate ATP . Structure The structure of these chaperonins resemble two donuts stacked on top of one another to create a barrel. Each ring is composed of either 7, 8 or 9 subunits depending on the organism in which the chaperonin is found. Categories of chaperonins Group I Group I chaperonins are found in bacteria as well as organelles of endosymbiotic origin chloroplasts and mitochondria . The GroEL GroES complex in E. coli is a Group I chaperonin and the best characterized large 1 MDa chaperonin complex. GroEL is a double ring 14mer with a greasy hydrophobic patch at its opening and can accommodate the native folding of substrates 15 60 kDa in size. GroES is a single ring heptamer that binds to GroEL in the presence of ATP or transition state analogues of ATP hydrolysis, such as ADP AlF sub 3 sub . It s like a cover that covers GroEL box bottle . GroEL GroES may not be able to undo protein aggregates, but kinetically it competes in the pathway of misfolding and aggregation, thereby preventing aggregate formation. ref name pmid14686103 cite journal author Fenton WA, Horwich AL title Chaperonin mediated protein folding fate of substrate polypeptide journal Q. Rev. Biophys. volume 36 issue 2 pages 229 56 year 2003 month May pmid 14686103 doi 10.1017 S0033583503003883 url ref Group II Group II chaperonins, found in the eukaryotic cytosol and in archaea , are more poorly characterized. TRiC TCP 1 Ring Complex, also called CCT for chaperonin containing TCP 1 , the eukaryotic chaperonin, is composed of eight diffe ... more details
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- Hemolysin
merge from Haemolysin A date June 2011 merge from Haemolysin E date June 2011 Pfam box Symbol Leukocidin Name image 7ahl opm.gif width 250 caption Alpha hemolysin, a transmembrane heptamer Pfam PF07968 InterPro IPR001340 SMART Prosite SCOP TCDB OPM family 35 OPM protein 7ahl PDB PDB3 1t5r H 57 303 PDB3 1lkf A 60 310 PDB3 2lkf A 60 310 PDB3 3lkf A 60 310 PDB3 1pvl 58 308 PDB3 7ahl G 62 314 Infobox protein family Symbol Hemolysin N Name Hemolytic toxin N terminal image width caption crystal structure of the vibrio cholerae cytolysin hlya pro toxin with octylglucoside bound Pfam PF12563 Pfam clan InterPro IPR022220 SMART PROSITE MEROPS SCOP TCDB OPM family OPM protein CAZy CDD Hemolysins are exotoxins produced by bacteria that cause lysis of red blood cells in vitro . Visualization of hemolysis of red blood cells in agar plates facilitates the categorization of some pathogenic bacteria such as Streptococcus and Staphylococcus . Although the lytic activity of some hemolysins on red blood cells may be important for nutrient acquisition or for causing certain conditions such as anemia, many hemolysin producing pathogens do not cause significant lysis of red blood cells during infection. Although hemolysins are able to lyse red blood cells in vitro , the ability of hemolysins to target other cells, including white blood cell s, often accounts for the effects of hemolysins in the host. Most hemolysins are proteins, but others such as rhamnolipid s are lipid biosurfactant s. ref name pmid16199139 cite journal author Stipcevic T, Piljac T, Isseroff RR title Di rhamnolipid from Pseudomonas aeruginosa displays differential effects on human keratinocyte and fibroblast cultures journal J. Dermatol. Sci. volume 40 issue 2 pages 141 3 year 2005 month November pmid 16199139 pmc 1592130 doi 10.1016 j.jdermsci.2005.08.005 url ref Function Bacteria may use hemolysins as a way to obtain nutrients from host cells. For example, iron may be a limiting factor in the growth of various pathog ... more details
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- CLPP
PBB geneid 8192 ATP dependent Clp protease proteolytic subunit is an enzyme that in humans is encoded by the CLPP gene . ref name pmid8543061 cite journal author Bross P, Andresen BS, Knudsen I, Kruse TA, Gregersen N title Human ClpP protease cDNA sequence, tissue specific expression and chromosomal assignment of the gene journal FEBS Lett volume 377 issue 2 pages 249 52 year 1996 month Feb pmid 8543061 pmc doi 10.1016 0014 5793 95 01353 9 ref ref name entrez cite web title Entrez Gene CLPP ClpP caseinolytic peptidase, ATP dependent, proteolytic subunit homolog E. coli url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 8192 accessdate ref It is found in mitochondria and is widely distributed in Bacteria bacterial species. In several bacteria, such as Escherichia coli E. coli , proteins tagged with the SsrA peptide ANDENYALAA encoded by Transfer messenger RNA tmRNA are digested by Clp proteases. ref name pmid9573050 cite journal doi 10.1101 gad.12.9.1338 author Gottesman S, Roche E, Zhou Y, Sauer RT title The ClpXP and ClpAP proteases degrade proteins with carboxy terminal peptide tails added by the SsrA tagging system journal Genes Dev volume 12 issue 9 pages 1338 47 year 1998 pmid 9573050 pmc 316764 ref The PBB Summary template is automatically maintained by Protein Box Bot. See Template PBB Controls to Stop updates. PBB Summary section title summary text The protein encoded by this gene belongs to the peptidase family S14 and hydrolyzes proteins into small peptides in the presence of ATP and magnesium. The protein is transported into mitochondrial matrix and is associated with the inner mitochondrial membrane. ref name entrez See also Protease Transfer messenger RNA References reflist Further reading refbegin 2 PBB Further reading citations cite journal author Kang SG, Dimitrova MN, Ortega J, et al. title Human mitochondrial ClpP is a stable heptamer that assembles into a tetradecamer in the presence of ClpX journal J. Biol. Chem. v ... more details
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- Protein quaternary structure
tetramer 5 pentamer 6 hexamer valign top 7 heptamer 8 octamer 9 nonamer 10 decamer 11 undecamer ... more details
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- V(D)J recombination
recombinase. RSSs are composed of seven conserved nucleotides a heptamer that reside next to the gene ... more details
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- PSME1
PA28 alpha is a heptamer journal Protein Sci. volume 6 issue 11 pages 2469 73 year 1998 pmid 9385652 ... more details
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- AB toxin
as a heptamer in the Cell membrane membrane . ref name pmid1910002 cite journal author Pezard ... more details
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- Transmembrane protein
?superfamily 34 MspA porin octamer, n S 16 and hemolysin heptamer n S 14 http opm.phar.umich.edu ... more details
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- GroES
co chaperonin heptamer residues disrupting oligomeric unfolded state identified journal BMC ... more details
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- Chaperone (protein)
heptamer that binds to GroEL in the presence of ATP or ADP. GroEL GroES may not be able to undo ... more details
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- Apoptosome
pathway of apoptosis . ref name Ceconi The wheel shaped Heptamer heptameric complex with sevenfold ... more details
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- Anthrax
access to the interior of the host cell. The acidified environment within the endosome triggers the heptamer ... more details
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