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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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Isidro A, Santos MA, Henriques AO, Tavares P (2004b) The high-resolution functional map of bacteriophage SPP1 portal protein. Mol Microbiol 51:949–962 Draw the resultant from the tail of the first vector to the head of the last vector. Label this vector as Resultant or simply R. 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 Olia AS, Al-Bassam J, Winn-Stapley DA, Joss L, Casjens SR, Cingolani G (2006) Binding-induced stabilization and assembly of the phage P22 tail accessory factor gp4. J Mol Biol 363:558–576

Auzat I, Petitpas I, Lurz R, Weise F, Tavares P (2014) A touch of glue to complete bacteriophage assembly: the tail-to-head joining protein (THJP) family. Mol Microbiol 91:1164–1178 Parker ML, Eiserling FA (1983) Bacteriophage SPO1 structure and morphogenesis. I. Tail structure and length regulation. J Virol 46:239–249 Maxwell KL, Davidson AR, Murialdo H, Gold M (2000) Thermodynamic and functional characterization of protein W from bacteriophage lambda. The three C-terminal residues are critical for activity. J Biol Chem 275:18879–18886 Thomas JO (1974) Chemical linkage of the tail to the right-hand end of bacteriophage lambda DNA. J Mol Biol 87:1–9 Using the BAP complex facilitates orientation determination in EM reconstruction, as previously observed for ClpA-ClpP ( Effantin et al., 2010). Side views of the elongated BAP-ClpP complex are easily recognisable ( Figure 1B) whereas in 2D projections of ClpB alone, which has a globular shape, it is hard to distinguish side from tilted views. By restricting the dataset to side views the angle assignment is more reliable, and these views are sufficient to generate the full 3D structure ( Figure 1C). Using H/D exchange experiments, which report on the solvent accessibility and structural flexibility of amide hydrogens, we found that BAP, either alone or bound to ClpP, displays the same protection pattern as ClpB, implying the same MD conformation ( Figure 1—figure supplement 1).Trus BL, Cheng N, Newcomb WW, Homa FL, Brown JC, Steven AC (2004) Structure and polymorphism of the UL6 portal protein of herpes simplex virus type 1. J Virol 78:12668–12671 Cardarelli L, Maxwell KL, Davidson AR (2011) Assembly mechanism is the key determinant of the dosage sensitivity of a phage structural protein. Proc Natl Acad Sci U S A 108:10168–10173 van Heel M, Orlova EV, Dube P, Tavares P (1996) Intrinsic versus imposed curvature in cyclical oligomers: the portal protein of bacteriophage SPP1. EMBO J 15:4785–4788 Chen DH, Baker ML, Hryc CF, DiMaio F, Jakana J, Wu W, Dougherty M, Haase-Pettingell C, Schmid MF, Jiang W, Baker D, King JA, Chiu W (2011) Structural basis for scaffolding-mediated assembly and maturation of a dsDNA virus. Proc Natl Acad Sci U S A 108:1355–1360

Lengyel JA, Goldstein RN, Marsh M, Calendar R (1974) Structure of the bacteriophage P2 tail. Virology 62:161–174 It has become clear that AAA+ proteins are highly dynamic molecular motors unlikely to exist in a homogeneous structural state. Therefore we generated asymmetric reconstructions of ClpB. Although the resolution of the asymmetric structures is not sufficient to support a detailed mechanistic model, these reconstructions provide the first visualization of the MD conformational flexibility that was inferred from biochemical analysis ( Lee et al., 2003; Haslberger et al., 2007; Oguchi et al., 2012). The asymmetric structures show that the MD orientation varies around the ring occupying the repressed, wild type-like and hyperactive positions described by the symmetrised averages. The variable tilts of MDs observed around the ring suggest that 2 to 4 adjacent subunits are available for DnaK binding in the wild-type vs only 1 in the repressed mutant ( Figure 6B,C). This is consistent with the estimated stoichiometry of 2–5 molecules of DnaK per ClpB hexamer required for activation ( Seyffer et al., 2012; Desantis et al., 2014). It also suggests that at least four subunits must have detached MDs to allow activity, perhaps through movements of the AAA+ domains, in agreement with the number of ClpX subunits that hydrolyze ATP in a coordinated manner to unfold GFP in single molecule experiments ( Sen et al., 2013). Moreover, we calculated an ADP binding stoichiometry of 4 for both wild type and mutants ( Figure 6—figure supplement 3), which indicates that although ATP hydrolysis is strongly affected, detachment of the MD does not change the nucleotide binding. The result of adding 11 km, north plus 11 km, east is a vector with a magnitude of 15.6 km. Later, the method of determining the direction of the vector will be discussed. The differences between the mutant structures were tested by refining with interchanged starting models. In both cases, the original mutant structure was recovered despite the use of the other map as a starting model for projection matching ( Figure 3—figure supplement 1).Davidson AR, Cardarelli L, Pell LG, Radford DR, Maxwell KL (2012) Long noncontractile tail machines of bacteriophages. Adv Exp Med Biol 726:115–142 Chattoraj DK, Inman RB (1974) Location of DNA ends in P2, 186, P4 and lambda bacteriophage heads. J Mol Biol 87:11–22

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