1WDY

Crystal structure of ribonuclease

Summary for 1WDY

• Entry DOI: 10.2210/pdb1wdy/pdb
• Descriptor: 2-5A-dependent ribonuclease, 5'-O-MONOPHOSPHORYLADENYLYL(2'->5')ADENYLYL(2'->5')ADENOSINE (3 entities in total)
• Functional Keywords: hydrolase, nuclease, rna-binding
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: Q05823
• Total number of polymer chains: 1
• Total formula weight: 32182.42

Authors

Tanaka, N.,Nakanishi, M.,Kusakabe, Y.,Goto, Y.,Kitade, Y.,Nakamura, K.T. (deposition date: 2004-05-19, release date: 2004-10-05, Last modification date: 2024-11-20)

Primary citation

Tanaka, N.,Nakanishi, M.,Kusakabe, Y.,Goto, Y.,Kitade, Y.,Nakamura, K.T.
Structural basis for recognition of 2',5'-linked oligoadenylates by human ribonuclease L
Embo J., 23:3929-3938, 2004

PubMed Abstract: An interferon-induced endoribonuclease, ribonuclease L (RNase L), is implicated in both the molecular mechanism of action of interferon and the fundamental control of RNA stability in mammalian cells. RNase L is catalytically active only after binding to an unusual activator molecule containing a 5'-phosphorylated 2',5'-linked oligoadenylate (2-5A), in the N-terminal half. Here, we report the crystal structure of the N-terminal ankyrin repeat domain (ANK) of human RNase L complexed with the activator 2-5A. This is the first structural view of an ankyrin repeat structure directly interacting with a nucleic acid, rather than with a protein. The ANK domain folds into eight ankyrin repeat elements and forms an extended curved structure with a concave surface. The 2-5A molecule is accommodated at a concave site and directly interacts with ankyrin repeats 2-4. Interestingly, two structurally equivalent 2-5A binding motifs are found at repeats 2 and 4. The structural basis for 2-5A recognition by ANK is essential for designing stable 2-5As with a high likelihood of activating RNase L.

PubMed: 15385955
DOI: 10.1038/sj.emboj.7600420

Experimental method

X-RAY DIFFRACTION (1.8 Å)