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2JRC

Solution structure of Peptidyl-tRNA Hydrolase from Mycobacterium tuberculosis H37Rv.

2JRC の概要
エントリーDOI10.2210/pdb2jrc/pdb
分子名称Peptidyl-tRNA hydrolase (1 entity in total)
機能のキーワードpth, solution structure, mycobacterium tuberculosis h37rv, hydrolase
由来する生物種Mycobacterium tuberculosis
細胞内の位置Cytoplasm (By similarity): P65865
タンパク質・核酸の鎖数1
化学式量合計22012.26
構造登録者
Pulavarti, S.V.S.R.K.,Jain, A.,Pathak, P.P.,Arora, A. (登録日: 2007-06-22, 公開日: 2008-05-27, 最終更新日: 2023-12-20)
主引用文献Pulavarti, S.V.,Jain, A.,Pathak, P.P.,Mahmood, A.,Arora, A.
Solution structure and dynamics of peptidyl-tRNA hydrolase from Mycobacterium tuberculosis H37Rv.
J.Mol.Biol., 378:165-177, 2008
Cited by
PubMed Abstract: Eubacterial peptidyl-tRNA hydrolase is an essential enzyme that hydrolyzes peptidyl-tRNAs that are released into the cytoplasm because of premature termination of translation, expression of minigenes, and action of lincosamide and macrolide antibiotics. This averts the arrest of protein synthesis caused by depletion of free tRNA. Recently, we demonstrated that Mycobacterium tuberculosis peptidyl-tRNA hydrolase (MtPth) is present in the cytosol of mycobacterium and is capable of hydrolyzing peptidyl-tRNA. Here, we present the solution structure of MtPth, which is the first solution structure for this family of proteins. MtPth typically consists of seven-stranded mixed beta-sheet surrounded by six alpha-helices. The backbone dynamics for this enzyme were probed by measuring (15)N relaxation parameters and these were analyzed with model-free formalism and reduced spectral density mapping analysis. Overall, the protein molecule has tau(m) of 9.67+/-0.02 ns. The (15)N relaxation data analysis reveals that while majority of the protein backbone is rigid to motions, a short segment consisting of enzymatically critical residue H22, the loop-helix cover over the active site crevice, and the C-terminal helical hairpin exhibit motions on the milli-to microsecond timescale, all of which are linked to interaction with the substrate peptidyl-tRNA.
PubMed: 18342886
DOI: 10.1016/j.jmb.2008.02.027
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 2jrc
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-07-30に公開中

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