1PYV

NMR solution structure of the mitochondrial F1b presequence peptide from Nicotiana plumbaginifolia

1PYV の概要

• エントリーDOI: 10.2210/pdb1pyv/pdb
• 分子名称: ATP synthase beta chain, mitochondrial precursor (1 entity in total)
• 機能のキーワード: hydrolase
• 由来する生物種: Nicotiana plumbaginifolia (curled-leaved tobacco)
• 細胞内の位置: Mitochondrion: P17614
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 5753.66

構造登録者

Moberg, P.,Nilsson, S.,Stahl, A.,Eriksson, A.C.,Glaser, E.,Maler, L. (登録日: 2003-07-09, 公開日: 2004-04-06, 最終更新日: 2024-05-22)

主引用文献

Moberg, P.,Nilsson, S.,Stahl, A.,Eriksson, A.C.,Glaser, E.,Maler, L.
NMR solution structure of the mitochondrial F1beta presequence from Nicotiana plumbaginifolia
J.Mol.Biol., 336:1129-1140, 2004

PubMed Abstract: We have isolated, characterized and determined the three-dimensional NMR solution structure of the presequence of ATPsynthase F1beta subunit from Nicotiana plumbaginifolia. A general method for purification of presequences is presented. The method is based on overexpression of a mutant precursor containing a methionine residue introduced at the processing site, followed by CNBr-cleavage and purification of the presequence on a cation-exchange column. The F1beta presequence, 53 amino acid residues long, retained its native properties as evidenced by inhibition of in vitro mitochondrial import and processing at micromolar concentrations. CD spectroscopy revealed that the F1beta presequence formed an alpha-helical structure in membrane mimetic environments such as SDS and DPC micelles (approximately 50% alpha-helix), and in acidic phospholipid bicelles (approximately 60% alpha-helix). The NMR solution structure of the F1beta presequence in SDS micelles was determined on the basis of 518 distance and 21 torsion angle constraints. The structure was found to contain two helices, an N-terminal amphipathic alpha-helix (residues 4-15) and a C-terminal alpha-helix (residues 43-53), separated by a largely unstructured 27 residue long internal domain. The N-terminal amphipathic alpha-helix forms the putative Tom20 receptor binding site, whereas the C-terminal alpha-helix is located upstream of the mitochondrial processing peptidase cleavage site.

PubMed: 15037074
DOI: 10.1016/j.jmb.2004.01.006

実験手法

SOLUTION NMR