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8FA3

Structure of N-terminal of Schistosoma japonicum asparaginyl-tRNA synthetase

8FA3 の概要
エントリーDOI10.2210/pdb8fa3/pdb
NMR情報BMRB: 31060
分子名称Asparagine--tRNA ligase (1 entity in total)
機能のキーワードbeta-hairpin, n-terminal extension, intrinsically disordered region, ligase
由来する生物種Schistosoma japonicum
タンパク質・核酸の鎖数1
化学式量合計13576.25
構造登録者
Peck, Y.,Daly, N.L.,Mobli, M. (登録日: 2022-11-25, 公開日: 2023-09-06, 最終更新日: 2024-09-25)
主引用文献Peck, Y.,Pickering, D.,Mobli, M.,Liddell, M.J.,Wilson, D.T.,Ruscher, R.,Ryan, S.,Buitrago, G.,McHugh, C.,Love, N.C.,Pinlac, T.,Haertlein, M.,Kron, M.A.,Loukas, A.,Daly, N.L.
Solution structure of the N-terminal extension domain of a Schistosoma japonicum asparaginyl-tRNA synthetase.
J.Biomol.Struct.Dyn., 42:7934-7944, 2024
Cited by
PubMed Abstract: Several secreted proteins from helminths (parasitic worms) have been shown to have immunomodulatory activities. Asparaginyl-tRNA synthetases are abundantly secreted in the filarial nematode (AsnRS) and the parasitic flatworm (AsnRS), indicating a possible immune function. The suggestion is supported by AsnRS alleviating disease symptoms in a T-cell transfer mouse model of colitis. This immunomodulatory function is potentially related to an N-terminal extension domain present in eukaryotic AsnRS proteins but few structure/function studies have been done on this domain. Here we have determined the three-dimensional solution structure of the N-terminal extension domain of AsnRS. A protein containing the 114 N-terminal amino acids of AsnRS was recombinantly expressed with isotopic labelling to allow structure determination using 3D NMR spectroscopy, and analysis of dynamics using NMR relaxation experiments. Structural comparisons of the N-terminal extension domain of AsnRS with filarial and human homologues highlight a high degree of variability in the β-hairpin region of these eukaryotic N-AsnRS proteins, but similarities in the disorder of the C-terminal regions. Limitations in PrDOS-based intrinsically disordered region (IDR) model predictions were also evident in this comparison. Empirical structural data such as that presented in our study for N-AsnRS will enhance the prediction of sequence-homology based structure modelling and prediction of IDRs in the future.Communicated by Ramaswamy H. Sarma.
PubMed: 37572327
DOI: 10.1080/07391102.2023.2241918
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 8fa3
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件を2026-02-04に公開中

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