Literature summary for 3.1.26.4 extracted from

Shaban, N.M.; Harvey, S.; Perrino, F.W.; Hollis, T.
The structure of the mammalian RNase H2 complex provides insight into RNA.NA hybrid processing to prevent immune dysfunction (2010), J. Biol. Chem., 285, 3617-3624.

Crystallization (Commentary)

Crystallization (Comment)	Organism
heterotrimeric complex of the RNase H2A, RNase H2B, and RNase H2C proteins, to 3.1 A resolution. The overall structure reveals an elongated arrangement of the subunits with the H2C protein in the middle flanked by the H2A and H2B proteins on the ends. Construction of a model for an Okazaki fragment binding to the mouse RNase H2 complex. In the model, the double-stranded RNA-DNA molecule runs through the active site cleft and is positioned to make several favorable electrostatic interactions and no significant steric clashes with the protein. The RNA-DNA hybrid is situated so that the target phosphodiester bond is in the proper orientation for nucleophile attack initiated by a two-metal ion chemistry	Mus musculus

Crystallization (Comment)

Organism

heterotrimeric complex of the RNase H2A, RNase H2B, and RNase H2C proteins, to 3.1 A resolution. The overall structure reveals an elongated arrangement of the subunits with the H2C protein in the middle flanked by the H2A and H2B proteins on the ends. Construction of a model for an Okazaki fragment binding to the mouse RNase H2 complex. In the model, the double-stranded RNA-DNA molecule runs through the active site cleft and is positioned to make several favorable electrostatic interactions and no significant steric clashes with the protein. The RNA-DNA hybrid is situated so that the target phosphodiester bond is in the proper orientation for nucleophile attack initiated by a two-metal ion chemistry

Mus musculus

Protein Variants

Protein Variants	Comment	Organism
D142N	mutation in strictly positionally conserved acidic residues, complete loss of activity	Mus musculus
D170N	mutation in strictly positionally conserved acidic residues, complete loss of activity	Mus musculus
D34N	mutation in strictly positionally conserved acidic residues, complete loss of activity	Mus musculus
E35A	mutation in strictly positionally conserved acidic residues, complete loss of activity	Mus musculus
G37S	mutation in subunit H2A identified in patients with Aicardi-Goutieres' syndrome. Mutation appears to distort the active site accounting for the demonstrated substrate specificity modification	Mus musculus

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	Q9CWY8	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
Endonucleolytic cleavage to a 5'-phosphomonoester	active site geometry suggests a two-metal ion-dependent catalytic mechanism	Mus musculus	a

Subunits

Subunits	Comment	Organism
trimer	heterotrimeric complex of the RNase H2A, RNase H2B, and RNase H2C proteins, crystallization data	Mus musculus