Literature summary for 3.1.13.1 extracted from

Frazao, C.; McVey, C.E.; Amblar, M.; Barbas, A.; Vonrhein, C.; Arraiano, C.M.; Carrondo, M.A.
Unravelling the dynamics of RNA degradation by ribonuclease II and its RNA-bound complex (2006), Nature, 443, 110-114.

Cloned(Commentary)

Cloned (Comment)	Organism
X-ray crystallographic structures of both the ligand-free (at 2.44 A resolution) and RNA-bound (at 2.74 A resolution) forms of RNase II. Structures show that RNase II is organized into four domains: two cold-shock domains, one RNB catalytic domain, which has an unprecedented alphabeta-fold, and one S1 domain. The active site is buried within the RNB catalytic domain, in a pocket formed by four conserved sequence motifs. The structure shows that the catalytic pocket is only accessible to single-stranded RNA, and explains the specificity for RNA versus DNA cleavage. It also explains the dynamic mechanism of RNA degradation by providing the structural basis for RNA translocation and enzyme processivity	Escherichia coli

Cloned (Comment)

Organism

X-ray crystallographic structures of both the ligand-free (at 2.44 A resolution) and RNA-bound (at 2.74 A resolution) forms of RNase II. Structures show that RNase II is organized into four domains: two cold-shock domains, one RNB catalytic domain, which has an unprecedented alphabeta-fold, and one S1 domain. The active site is buried within the RNB catalytic domain, in a pocket formed by four conserved sequence motifs. The structure shows that the catalytic pocket is only accessible to single-stranded RNA, and explains the specificity for RNA versus DNA cleavage. It also explains the dynamic mechanism of RNA degradation by providing the structural basis for RNA translocation and enzyme processivity

Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P30850	-	-

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Release 2023.1 (January 2023)