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Crystal structure of the ligand‐binding form of nanoRNase from Bacteroides fragilis , a member of the DHH/DHHA1 phosphoesterase family of proteins
Author(s) -
Uemura Yuri,
Nakagawa Noriko,
Wakamatsu Taisuke,
Kim Kwang,
Montelione Gaetano Thomas,
Hunt John Francis,
Kuramitsu Seiki,
Masui Ryoji
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.06.053
Subject(s) - crystal structure , chemistry , rna , nucleotide , crystallography , stereochemistry , biology , biochemistry , gene
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.