Mueser T C, Nossal N G, Hyde C C
Laboratory of Structural Biology Research, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland 20892-2755, USA.
Cell. 1996 Jun 28;85(7):1101-12. doi: 10.1016/s0092-8674(00)81310-0.
Bacteriophage T4 RNase H is a 5' to 3' exonuclease that removes RNA primers from the lagging strand of the DNA replication fork and is a member of the RAD2 family of eukaryotic and prokaryotic replication and repair nucleases. The crystal structure of the full-length native form of T4 RNase H has been solved at 2.06 angstroms resolution in the presence of Mg2+ but in the absence of nucleic acids. The most conserved residues are clustered together in a large cleft with two Mg2+ in the proposed active site. This structure suggests the way in which the widely separated conserved regions in the larger nucleotide excision repair proteins, such as human XPG, could assemble into a structure like that of the smaller replication nucleases.
噬菌体T4核糖核酸酶H是一种5'至3'核酸外切酶，可从DNA复制叉的滞后链上去除RNA引物，它是真核和原核复制及修复核酸酶的RAD2家族成员。T4核糖核酸酶H全长天然形式的晶体结构已在存在Mg2+但不存在核酸的情况下以2.06埃的分辨率解析出来。最保守的残基聚集在一个大裂缝中，在假定的活性位点有两个Mg2+。这种结构表明，较大的核苷酸切除修复蛋白（如人类XPG）中广泛分离的保守区域可能组装成类似较小复制核酸酶的结构的方式。
