3CTR

Crystal structure of the RRM-domain of the poly(A)-specific ribonuclease PARN bound to m7GTP

Summary for 3CTR

• Entry DOI: 10.2210/pdb3ctr/pdb
• Descriptor: Poly(A)-specific ribonuclease PARN, 7-METHYL-GUANOSINE-5'-TRIPHOSPHATE (3 entities in total)
• Functional Keywords: parn, protein-rna-complex, m7g-cap, m7gtp, rna recognition motif, rrm, exonuclease, hydrolase, magnesium, metal-binding, nonsense-mediated mrna decay, nuclease, nucleus, phosphoprotein, rna-binding
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus : O95453
• Total number of polymer chains: 1
• Total formula weight: 12360.39

Authors

Monecke, T.,Schell, S.,Dickmanns, A.,Ficner, R. (deposition date: 2008-04-14, release date: 2008-07-29, Last modification date: 2024-02-21)

Primary citation

Monecke, T.,Schell, S.,Dickmanns, A.,Ficner, R.
Crystal structure of the RRM domain of poly(A)-specific ribonuclease reveals a novel m(7)G-cap-binding mode.
J.Mol.Biol., 382:827-834, 2008

PubMed Abstract: Poly(A)-specific ribonuclease (PARN) is a processive 3'-exoribonuclease involved in the decay of eukaryotic mRNAs. Interestingly, PARN interacts not only with the 3' end of the mRNA but also with its 5' end as PARN contains an RRM domain that specifically binds both the poly(A) tail and the 7-methylguanosine (m(7)G) cap. The interaction of PARN with the 5' cap of mRNAs stimulates the deadenylation activity and enhances the processivity of this reaction. We have determined the crystal structure of the PARN-RRM domain with a bound m(7)G triphosphate nucleotide, revealing a novel binding mode for the m(7)G cap. The structure of the m(7)G binding pocket is located outside of the canonical RNA-binding surface of the RRM domain and differs significantly from that of other m(7)G-cap-binding proteins. The crystal structure also shows a remarkable conformational flexibility of the RRM domain, leading to a perfect exchange of two alpha-helices with an adjacent protein molecule in the crystal lattice.

PubMed: 18694759
DOI: 10.1016/j.jmb.2008.07.073

Experimental method

X-RAY DIFFRACTION (2.1 Å)