期刊
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
卷 81, 期 10, 页码 1840-1846出版社
WILEY
DOI: 10.1002/prot.24306
关键词
aspartyl-tRNA synthetase; multi-tRNA synthetase complex; N-helix; crystal structure
资金
- Ministry of Education, Science and Technology (MEST), Republic of Korea through the National Research Foundation [2012-054237]
- National Cancer Center, Republic of Korea [1120170]
- Korea Health Promotion Institute [1120170] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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 angstrom. DRS is a homodimer with a dimer interface of 3750.5 angstrom(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 1. 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. (c) 2013 Wiley Periodicals, Inc.
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