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Crystal structure of human cytosolic aspartyl‐tRNA synthetase, a component of multi‐tRNA synthetase complex
Author(s) -
Kim Kyung Rok,
Park Sang Ho,
Kim Hyoun Sook,
Rhee Kyung Hee,
Kim ByungGyu,
Kim Dae Gyu,
Park Mi Seul,
Kim HyunJung,
Kim Sunghoon,
Han Byung Woo
Publication year - 2013
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.24306
Subject(s) - transfer rna , dimer , biochemistry , elongation factor , aspartic acid , amino acid , cytosol , chemistry , enzyme , phosphorylation , helix (gastropod) , monomer , stereochemistry , biology , rna , gene , ribosome , organic chemistry , polymer , ecology , snail
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 Å 2 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 tRNA Asp 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.