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==Relevance==
==Relevance==
[[Image:Image_7_(1).png|300px|right|thumb|'''Figure 3:'''Sequence alignment of NrdH from ''Mycobacterium tuberculosis'', ''Corynebacterium glutamicum'', and ''Echerichia coli''. The thioredoxin fold found in NrdH of ''M. tuberculosis''and it is similar to NrdH of other organisms.]]
[[Image:Image_7_(1).png|300px|right|thumb|'''Figure 3:'''Sequence alignment of NrdH from ''Mycobacterium tuberculosis'', ''Corynebacterium glutamicum'', and ''Echerichia coli''. The thioredoxin fold is found in NrdH of ''M. tuberculosis'', and it is similar to NrdH of other organisms.]]
NrdH of ''M. tuberculosis'' has a thioredoxin fold, which was predicted due to the fact that NrdH of other organisms have a similar thioredoxin fold. This was shown by superimposing the structure of NrdH of multiple organisms. These superimpositions are important because it allows for analyzation of the similarities and differences of NrdH of ''M. tuberculosis'' with glutaredoxin and thioredoxin. There are slight changes in the series of sequence which in turn leads to a change in the tertiary structure. In the process of modeling NrdH with the glutaredoxin-1b RNR C-terminal peptide complex, it was apparent that the peptide bonds were slightly different within the class 1b RNRs. This also provided more evidence for the specificity of NrdH to NrdE. Genes that encode for NrdE and NrdF are essential for growth, and RR might be an attractive biochemical pathway for antimycobacterial drug discovery. Organisms that depend solely on class 1b RNR could potentially contain the essential genes and serve as potential drug targets for treating tuberculosis <ref name="Phulera" />.
NrdH of ''M. tuberculosis'' has a thioredoxin fold, which was predicted due to the fact that NrdH of other organisms have a similar thioredoxin fold. This was shown by superimposing the structure of NrdH of multiple organisms. These superimpositions are important because it allows for analyzation of the similarities and differences of NrdH of ''M. tuberculosis'' with glutaredoxin and thioredoxin. There are slight changes in the series of sequence which in turn leads to a change in the tertiary structure. In the process of modeling NrdH with the glutaredoxin-1b RNR C-terminal peptide complex, it was apparent that the peptide bonds were slightly different within the class 1b RNRs. This also provided more evidence for the specificity of NrdH to NrdE. Genes that encode for NrdE and NrdF are essential for growth, and RR might be an attractive biochemical pathway for antimycobacterial drug discovery. Organisms that depend solely on class 1b RNR could potentially contain the essential genes and serve as potential drug targets for treating tuberculosis <ref name="Phulera" />.


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OCA, Vija Kasniunas, Bryant H. Dawson, Nicole Bledsoe, Geoffrey C. Hoops, Natalie Van Ochten