Literature summary for 3.1.13.1 extracted from

Zuo, Y.; Vincent, H.A.; Zhang, J.; Wang, Y.; Deutscher, M.P.; Malhotra, A.
Structural basis for processivity and single-strand specificity of RNase II (2006), Mol. Cell, 24, 149-156.

Crystallization (Commentary)

Crystallization (Comment)	Organism
three RNA-binding domains come together to form a clamp-like assembly, which can only accommodate single stranded RNA. This leads into a narrow, basic channel that ends at the putative catalytic center that is completely enclosed within the body of the protein. The putative path for RNA agrees well with biochemical data indicating that a 3' single strand overhang of 7-10 nt is necessary for binding and hydrolysis by RNase II. The presence of the clamp and the narrow channel provides an explanation for the processivity of RNase II and for why its action is limited to single stranded RNA	Escherichia coli

Crystallization (Comment)

Organism

three RNA-binding domains come together to form a clamp-like assembly, which can only accommodate single stranded RNA. This leads into a narrow, basic channel that ends at the putative catalytic center that is completely enclosed within the body of the protein. The putative path for RNA agrees well with biochemical data indicating that a 3' single strand overhang of 7-10 nt is necessary for binding and hydrolysis by RNase II. The presence of the clamp and the narrow channel provides an explanation for the processivity of RNase II and for why its action is limited to single stranded RNA

Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)