4J15

Crystal structure of human cytosolic aspartyl-tRNA synthetase, a component of multi-tRNA synthetase complex

4J15 の概要

• エントリーDOI: 10.2210/pdb4j15/pdb
• 分子名称: Aspartate--tRNA ligase, cytoplasmic, GLYCEROL (3 entities in total)
• 機能のキーワード: aspartyl-trna synthetase, trna, ligase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: P14868
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 119505.63

構造登録者

Kim, K.R.,Park, S.H.,Kim, H.S.,Kim, B.-G.,Kim, D.G.,Rhee, K.H.,Park, M.S.,Kim, H.-J.,Kim, S.,Han, B.W. (登録日: 2013-02-01, 公開日: 2013-05-15, 最終更新日: 2023-11-08)

主引用文献

Kim, K.R.,Park, S.H.,Kim, H.S.,Rhee, K.H.,Kim, B.-G.,Kim, D.G.,Park, M.S.,Kim, H.-J.,Kim, S.,Han, B.W.
Crystal structure of human cytosolic aspartyl-tRNA synthetase, a component of multi-tRNA synthetase complex
Proteins, 81:1840-1846, 2013

PubMed 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 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.

PubMed: 23609930
DOI: 10.1002/prot.24306

実験手法

X-RAY DIFFRACTION (2.24 Å)