Category:Team Blue B

Sequence alignment via BlastP gave an E value of 1 E-12 and 68 % query cover. This gene can be homolog to phosphoadenylyl-sulfate reductase domain

Sequence alignment via BlastP gave an E value of 5E-34 and 84% query cover which showed the two genes have high possibility to be homologs

From table 1, the significant reduction of Vmax quantities in both the mutant Cys236Ser and the Tyr206Phe enzymes compared to the wild type Vmax suggests that wild type cysH protein reduces phosphoadenylyl-sulfate.

Figure 1 showed that ThyX proteins also act as NADPH oxidase by reacting directly with O2.

Figure 2 shows the aligned using ClustaIW and subjected to phylogenetic analysis. Both Analyses resulted in trees of the same topology.

The order of tail genes is highly conserved. The major tail protein gene is always upstream of the tape measure protein gene

Dephospho-CoA kinase was purified from C.ammoniagenes and cloned in E.Coli. Desphospho -CoA kinase activity was determined based on ADP formation. the kinetic constant for DCK showed by the ratio the change in concentration of ATP and DCK. Activity of DCK also were also at maximum rate when at pH ~ 8.5

Figure 1B in this reference showed that this entire gene was embedded within ply 187 gene by changing the reading frame near N terminus of ply187.

Figure 1B and 4 showed the present of Ply-Holin protein embedded at beginning of N terminus of this whole gene. The graphs showed the protein as hydrophobic beta turn linker, dual start motif stretch of hydrophobic amino acid. When tested this holin sequence in Ecoli, it caused well wall degradation. Mutation at at cys residue to lysine caused less damage to the cell.

Expression of a fragment ply187 gave only 297 aa chain which represent only 47% of the protein entire length. Individual lysis activity only different fragments of the gene were performed and showed that peptidoglycan hydrolyzing activity were highest at N termites of the protein. (Shown in figure 3)

The authors use linker insert mutant and frameshift on protease gene. As the results, (Shown in Fig 2) mutant genes are not able to perform proteolysis and protease requires specific spanning residues on the target polypeptide to incorporate into prohead.

The experiment shows that mutation at His residue within the gene cause inactive exonuclease.

Figure 2

Figure 1. show that the protein can complement the function of DNA K and DNA G.

The Author use table 1 to show that the protein can complement the function FtsK

The authors use linker insert mutant and frameshift on protease gene. As the results, (Shown in Fig 2) mutant genes are not able to perform proteolysis and protease requires specific spanning residues on the target polypeptide to incorporate into prohead.

The experiment shows that mutation at His residue within the gene cause inactive exonuclease.

The authors use mutations in both protease and portal complex to determine their roles in capsid assembly. Figures 2 and 5 show that inactivated portal protein does not give rise to correct capsid assembly and allow DNA packaging.