EC Number | Crystallization (Comment) | Organism |
---|---|---|
3.1.26.4 | annealed RNA and DNA dodecanucleotides complexed with RNase H, synthetic constructs, sitting drop vapor diffusion method at room temperature in conditions containing 20% PEG 3350, 0.2 M magnesium formate, 10% 2-methyl-2,4-pentanediol, X-ray diffraction structure determination and analysis, molecular replacement using the structure of Bacillus halodurans RNA-DNA component of the RNase H complex (PDB ID 1ZBI) as the search model | Halalkalibacterium halodurans |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.1.26.4 | Halalkalibacterium halodurans | - |
and synthetic constructs | - |
3.1.26.4 | Halalkalibacterium halodurans C-125 | - |
and synthetic constructs | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.26.4 | additional information | RNase (H)binding induces conformational changes in RNA-DNA hybrid. RNase H distorts the DNA strand of the hybrid by rotating the phosphodiester backbone around nucleotide dA6 about 5 A x02into the nucleotide binding pocket. The superimposition of the 2 RNA-DNA hybrids shows the RNA strand has a relatively similar conformation, but the DNA strand has been distorted to significantly widen the major groove of the helix. This flexibility of the DNA strand likely plays a role in substrate recognition and discrimination | Halalkalibacterium halodurans | ? | - |
? | |
3.1.26.4 | additional information | RNase (H)binding induces conformational changes in RNA-DNA hybrid. RNase H distorts the DNA strand of the hybrid by rotating the phosphodiester backbone around nucleotide dA6 about 5 A x02into the nucleotide binding pocket. The superimposition of the 2 RNA-DNA hybrids shows the RNA strand has a relatively similar conformation, but the DNA strand has been distorted to significantly widen the major groove of the helix. This flexibility of the DNA strand likely plays a role in substrate recognition and discrimination | Halalkalibacterium halodurans C-125 | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.1.26.4 | RNase H | - |
Halalkalibacterium halodurans |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.1.26.4 | additional information | conformational changes induced by RNase H binding of RNA:DNA heteroduplexes, crystal structure analysis of a dodecameric nonpolypurine/polypyrimidine tract RNA-DNA duplex and of the same sequence bound to RNase H, overview. The structural changes to the duplex include widening of the major groove to 12.5 A from 4.2 A and decrease in the degree of bending along the axis which may play a crucial role in the ribonucleotide recognition and cleavage mechanism within RNase H | Halalkalibacterium halodurans |
3.1.26.4 | physiological function | ribonucleotides within RNA-DNA hybrids are recognized and hydrolyzed by the RNase H enzymes | Halalkalibacterium halodurans |