2ID0

Escherichia coli RNase II

Summary for 2ID0

• Entry DOI: 10.2210/pdb2id0/pdb
• Descriptor: Exoribonuclease 2, MANGANESE (II) ION (3 entities in total)
• Functional Keywords: rnase, exoribonuclease, ribonuclease, exonuclease, nuclease, hydrolyase, mrna decay, rnr family, hydrolase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P30850
• Total number of polymer chains: 4
• Total formula weight: 293388.41

Authors

Zuo, Y.,Zhang, J.,Wang, Y.,Malhotra, A. (deposition date: 2006-09-13, release date: 2006-10-03, Last modification date: 2024-11-13)

Primary citation

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.
Mol.Cell, 24:149-156, 2006

PubMed Abstract: RNase II is a member of the widely distributed RNR family of exoribonucleases, which are highly processive 3'-->5' hydrolytic enzymes that play an important role in mRNA decay. Here, we report the crystal structure of E. coli RNase II, which reveals an architecture reminiscent of the RNA exosome. 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.

PubMed: 16996291
DOI: 10.1016/j.molcel.2006.09.004

Experimental method

X-RAY DIFFRACTION (2.35 Å)