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| == Function == | | == Function == |
| [https://www.uniprot.org/uniprot/Q64PD9_BACFR Q64PD9_BACFR] | | [https://www.uniprot.org/uniprot/Q64PD9_BACFR Q64PD9_BACFR] |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| 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.
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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.,Uemura Y, Nakagawa N, Wakamatsu T, Kim K, Montelione GT, Hunt JF, Kuramitsu S, Masui R FEBS Lett. 2013 Aug 19;587(16):2669-74. doi: 10.1016/j.febslet.2013.06.053. Epub , 2013 Jul 9. PMID:23851074<ref>PMID:23851074</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 3w5w" style="background-color:#fffaf0;"></div>
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
