Crystal structure of human cytosolic aspartyl‐tRNA synthetase,a component of multi‐tRNA synthetase complex |
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| Authors: | Hyoun Sook Kim Kyung Hee Rhee Byung‐Gyu Kim Dae Gyu Kim Mi Seul Park Hyun‐Jung Kim Sunghoon Kim Byung Woo Han |
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| Institution: | 1. Research Institute of Pharmaceutical Sciences, Department of Pharmacy, College of Pharmacy, Seoul National University, , Seoul, 151‐742 Korea;2. Medicinal Bioconvergence Research Center, Seoul National University, , Seoul, 151‐742 Korea;3. Department of Pharmacy, College of Pharmacy, Chung‐Ang University, , Seoul, 156‐756 Korea |
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| Abstract: | Human cytosolic aspartyl‐tRNA synthetase (DRS) catalyzes the attachment of the amino acid aspartic acid to its cognate tRNA and it is a component of the multi‐tRNA synthetase complex (MSC) which has been known to be involved in unexpected signaling pathways. Here, we report the crystal structure of DRS at a resolution of 2.25 Å. DRS is a homodimer with a dimer interface of 3750.5 Å2 which comprises 16.6% of the monomeric surface area. Our structure reveals the C‐terminal end of the N‐helix which is considered as a unique addition in DRS, and its conformation further supports the switching model of the N‐helix for the transfer of tRNAAsp to elongation factor 1α. From our analyses of the crystal structure and post‐translational modification of DRS, we suggest that the phosphorylation of Ser146 provokes the separation of DRS from the MSC and provides the binding site for an interaction partner with unforeseen functions.Proteins 2013; 81:1840–1846. © 2013 Wiley Periodicals, Inc. |
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| Keywords: | aspartyl‐tRNA synthetase multi‐tRNA synthetase complex N‐helix crystal structure |
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