The Learning Journey Match It - Head To Tail Puzzle Game For Kids - Helps Interactive Child Development, Problem-Solving and Social Skills - 20 Self-Correcting Puzzle Sets - For 3+ Years

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Chaban Y, Lurz R, Brasilès S, Cornilleau C, Karreman M, Zinn-Justin S, Tavares P, Orlova EV (2015) Structural rearrangements in the phage head-to-tail Interface during assembly and infection. Proc Natl Acad Sci U S A 112:7009–7014 Chang JT, Schmid MF, Haase-Pettingell C, Weigele PR, King JA, Chiu W (2010) Visualizing the structural changes of bacteriophage Epsilon15 and its Salmonella host during infection. J Mol Biol 402:731–740 Hu B, Margolin W, Molineux IJ, Liu J (2015) Structural remodeling of bacteriophage T4 and host membranes during infection initiation. Proc Natl Acad Sci U S A 112:E4919–E4928

Trus BL, Newcomb WW, Cheng N, Cardone G, Marekov L, Homa FL, Brown JC, Steven AC (2007) Allosteric signaling and a nuclear exit strategy: binding of UL25/UL17 heterodimers to DNA-Filled HSV-1 capsids. Mol Cell 26:479–489

Katsura I, Tsugita A (1977) Purification and characterization of the major protein and the terminator protein of the bacteriophage lambda tail. Virology 76:129–145 Guasch A, Pous J, Ibarra B, Gomis-Rüth FX, Valpuesta JM, Sousa N, Carrascosa JL, Coll M (2002) Detailed architecture of a DNA translocating machine: the high-resolution structure of the bacteriophages phi29 connector particle. J Mol Biol 315:663–676 The proximodistal principle is similar to the cephalocaudal principle, but instad of proceeding from top to bottom, it progresses from the center of the body outward. This means that development will start from core areas like arms, torso, and legs before branching out towards more peripheral areas such as fingers, toes, and face. For example, a baby might learn to sit up before they can roll over or crawl. The Proximodistal Principle Bazinet C, King J (1985) The DNA translocating vertex of dsDNA bacteriophage. Annu Rev Microbiol 39:109–129

Hu B, Margolin W, Molineux IJ, Liu J (2013) The bacteriophage T7 virion undergoes extensive structural remodeling during infection. Science 339:576–579 Step 5. To get the magnitude of the resultant, measure its length with a ruler. (Note that in most calculations, we will use the Pythagorean theorem to determine this length.) This is true for the addition of ordinary numbers as well—you get the same result whether you add \(\mathbf{\text{2}}+\mathbf{\text{3}}\) or \(\mathbf{\text{3}}+\mathbf{\text{2}}\), for example). We disagree that an ADP-bound subunit is more similar to an empty state than to an ATP-bound one. HX experiments of ClpB did not reveal differences in protection patterns in ADP and ATPγS, arguing that the conformations are similar [Oguchi, Y, et al, Nat Struct Mol Biol, 2012]. Importantly, both ADP and ATPγS binding led to substantial increase in HX protection compared to nucleotide-free ClpB oligomers, including Walker A motif regions. These data indicate that the overall conformational state of ADP-bound ClpB is more similar to the ATP-bound state than to the empty one. Thomas JO, Sternberg N, Weisberg R (1978) Altered arrangement of the DNA in injection-defective lambda bacteriophage. J Mol Biol 123:149–161

It is true that the ADP conformation does not support substrate and ClpP interaction. Both interactions are mediated by flexible loop structures located either at the central channel or at the bottom of the ClpB ring. Nucleotide-driven conformational changes of these mobile elements do not however necessarily reflect substantial conformational changes within the bulk of the AAA+ domains. In fact, soaking of ClpX crystals with either ATPγS, ATP or ADP led to comparable structural changes and ADP, presumably generated by residual hydrolysis, fits best the electron density of an ATPγS-soaked crystal [Glynn, SE, et al, Cell, 2009]. Notably, soaking of ClpX with nucleotides led to asymmetric binding, supporting a model in which ADP also binds asymmetrically to ClpB hexamers. Similarly, binding of either ATP, ATPγS or ADP to ClpX led to the same degree of FRET changes in an experimental setup monitoring the formation of “L” subunits, which show tighter interaction between the large and small subunit of the AAA domain [Stinson, BM, et al, Cell, 2013]. Together these data indicate that nucleotides, irrespective of their identity, cause similar overall structural changes in AAA+ domains. This work was supported by Canadian Institutes of Health Research (CIHR) grants (MOP‐126129, PJT‐152962, and FDN‐167277) to Mike Tyers; a Genome Canada Technology Development Platform Award to Mike Tyers and Pierre Thibault; a Wellcome Principal Research Fellowship (221044) to William C. Earnshaw; a CIHR Postdoctoral Fellowship to Daniel J. St‐Cyr; a Wellcome PhD Studentship (089396) to Florence H. Gohard; and a Canada Research Chair in Systems and Synthetic Biology to Mike Tyers. The authors would like to thank M.‐A. Poupart for insightful discussions regarding peptide and macrocycle synthesis, F. Galaud and S. Plamondon for technical support with peptide synthesis. Nováček J, Šiborová M, Benešík M, Pantůček R, Doškař J, Plevka P (2016) Structure and genome release of Twort-like Myoviridae phage with a double-layered baseplate. Proc Natl Acad Sci U S A 113:9351–9356 We think that nucleotide occupancy is likely to be similar between ADP and ATP states. Our calculated stoichiometries are in good agreement with numbers obtained for ClpX [Hersch, GL, et al, Cell, 2005], as each AAA domain of ClpB can bind four nucleotides.