Category:Team Syndicate

There is a 100% probability (e-value: 2e-164) that this sequence is homologous with ribonucleoside-diphosphate reductase large subunit found in Homo sapiens.

There is a 100% probability (e-value: 4e-164) that this sequence is homologous with ribonucleoside-diphosphate reductase large subunit found in Homo sapiens.

There is a 100% probability (e-value: 3e-164) that this sequence is homologous with ribonucleoside-diphosphate reductase large subunit found in Homo sapiens.

Fairman et al modeled different hexamer formations based on the crystal structures of two subunits of the ribonucleoside-diphosphate reductase complex and used Phaser (PMID:19461840) to model the hexamer holocomplex (see figure 4).

On HHPred, there is an 100% probability (8e-164 e-value) that this sequence is homologous with the ribonucleoside-diphosphate reductase gene found in humans.

Figure 3e shows the activity of wild-type ribonucleotide reductase relative to two mutant types which was determined using [3H]-CDP and [14C]-ADP reduction assays. ATP binds to the complex and activates it through an allosteric mechanism. This allows the ribonucleotide-diphosphate reductase complex to catalyze the formation of deoxyribonucleotides from ribonucleotides. The D16R mutant protein was not able to be activated by ATP at the allosteric site, and therefore had 45% reduced reductase activity (conversion of ADP to dADP). In the H2E mutant, the reductase activity relative to the wild-type was reduced by 44%.

Figure 4 shows BsDHFR activity as a function of reaction conditions through its pH dependence within MTEN buffer at different pH values and 40 °C with the rest at standard conditions. Optimum temperature for neutral pH of 7 was 75*C although enzyme stability was seen at pH 6.8 as a function of temperature due to very rapid loss of activity in the absence of substrate above 64 °C. pKa under standard assay was 7.5. The formation of THF is shown to be sensitive to pH since as pH increases, activity declines.

The three-dimensional structure of the dihydrofoate reductase (via X-ray crystallography) in Bacillus Stearothermophilus is iterated by Figure 3. This structure of Bacillus Stearothermophilus DHFR is the first monomeric DHFR structure from a thermophilic organism; there is also comparison between E. coli and T. maritima enzymes. IDA was used because this was the actual determination of the structure; the comparison to the other 2 enzymes helps support the functional conservation.

Fig.5B shows the presence of NDP kinase activity as followed by the formation of ADP resulting from phosphate transfer from ATP to dTDP. Also, in order to confirm that the enhanced NDP kinase activity measured in the extracts of bacteria transformed with pNDK was actually due to the protein encoded by the Gipl7 cDNA, Fig. 6A shows the enzime was partially purified and compared to its elution profile with that of the control extracts in Fig. 6B.

Blastp results showed the dihydrofolate reductase activity relating Bacillus anthracis and Bacillus Stearothermophilus with 100% identity, 100% query cover, and an e-value of 3.7E-37

Blastp results showed the dihydrofolate reductase activity relating Enterococcus faecalis and Bacillus Stearothermophilus with 100% identity, 100% query cover, and an e-value of 7.2E-39

Blastp results showed the dihydrofolate reductase activity relating Bacillus phage Coxiella burnetii and Bacillus Stearothermophilus with 100% identity, 100% query cover, and an e-value of 6.4E-38

The authors tested the effect of staphylococcus phage G1 gp67 on transcription of different types of bacteria. In figure 1 of the paper linked, it is shown that the addition of the protein gp67 inhibits the transcription of RNA in Staphylococcus aureus, but has no effect on the other bacteria tested upon.