Crystal structure of the ligand‐binding form of nanoRNase from Bacteroides fragilis, a member of the DHH/DHHA1 phosphoesterase family of proteins. Issue 16 (9th July 2013)

• Record Type: Journal Article
• Authors: Uemura, Yuri; Nakagawa, Noriko; Wakamatsu, Taisuke; Kim, Kwang; Montelione, Gaetano Thomas; Hunt, John Francis; Kuramitsu, Seiki; Masui, Ryoji
• Is Part Of: FEBS letters. Volume 587:Issue 16(2013)
• Page Start: 2669
• Page End: 2674
• Publication Date: 2013-07-09
• Subjects: Nrn -- nanoRNase -- bfNrn -- nanoRNase of Bacteroides fragilis -- shNrn -- nanoRNase of Staphylococcus haemolyticus -- ttNrn -- nanoRNase of Thermus thermophilus HB8 -- ttRecJ -- RecJ exonuclease of T. thermophilus HB8 -- pAp -- adenosine 3′, 5′-bisphosphate -- pGp -- guanosine 3′, 5′-bisphosphate -- nanoRNA -- nanoRNase -- DHH/DHHA1 family -- Crystal structure -- mRNA degradation; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1016/j.febslet.2013.06.053
• Languages: English
• ISSNs: 0014-5793

Abstract

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 Mn 2+ 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. Abstract : nanoRNase (Nrn) specifically degrades very short RNA in the mRNA degradation pathway. The crystal structure of Nrn complexed with a reaction product GMP was determined. Two Mn 2+ ions are coordinated by the DHH motif residues in the N‐terminal domain. GMP binds to the DHHA1 motif region in the C‐terminal domain. This structure enables us to predict the substrate‐bound form of Nrn.