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FEBS Lett. 2013 Aug 19;587(16):2669-74. doi: 10.1016/j.febslet.2013.06.053. Epub 2013 Jul 9.

Crystal structure of the ligand-binding form of nanoRNase from Bacteroides fragilis, a member of the DHH/DHHA1 phosphoesterase family of proteins.

Author information

1
Graduate School of Frontier Biosciences, Osaka University, Suita, Osaka 565-0871, Japan.

Abstract

NanoRNase (Nrn) specifically degrades nucleoside 3',5'-bisphosphate and the very short RNA, nanoRNA, during the final step of mRNA degradation. The crystal structure of Nrn in complex with a reaction product GMP was determined. The overall structure consists of two domains that are interconnected by a flexible loop and form a cleft. Two Mn²⁺ ions are coordinated by conserved residues in the DHH motif of the N-terminal domain. GMP binds near the DHHA1 motif region in the C-terminal domain. Our structure enables us to predict the substrate-bound form of Nrn as well as other DHH/DHHA1 phosphoesterase family proteins.

KEYWORDS:

Crystal structure; DHH/DHHA1 family; Nrn; RecJ exonuclease of T. thermophilus HB8; adenosine 3′,5′-bisphosphate; bfNrn; guanosine 3′,5′-bisphosphate; mRNA degradation; nanoRNA; nanoRNase; nanoRNase of Bacteroides fragilis; nanoRNase of Staphylococcus haemolyticus; nanoRNase of Thermus thermophilus HB8; pAp; pGp; shNrn; ttNrn; ttRecJ

PMID:
23851074
PMCID:
PMC4113422
DOI:
10.1016/j.febslet.2013.06.053
[Indexed for MEDLINE]
Free PMC Article

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