TY - JOUR
AU - Morikawa, K.
AB - THE three-dimensional structure of RNase H from Escherichia coli was determined at 1.8 Å resolution by X-ray crystallography. The enzyme was found to belong to the α + β class of structures, consisting of two distinct domains. The structure implies a possible region interacting with a DNA–RNA hybrid. The Mg2+-binding site essential for activity is located near a cluster of four acidic amino acids— one glutamic and three aspartic acid residues. These residues are completely conserved in the homology alignment of sequences of RNase H and reverse transcriptases from retro viruses and retrovirus-like entities1,2. The structural motif of β strands around the Mg2+-binding site has similarities to that in DNase I3–6. 
TI - Three-dimensional structure of ribonuclease H from E. coli
JF - Nature
DO - 10.1038/347306a0
DA - 1990-09-20
UR - https://www.deepdyve.com/lp/springer-journals/three-dimensional-structure-of-ribonuclease-h-from-e-coli-9R6EDEMGpR
SP - 306
EP - 309
VL - 347
IS - 6290
DP - DeepDyve
ER -