1ZFL

Solution structure of III-A, the major intermediate in the oxidative folding of leech carboxypeptidase inhibitor

1ZFL の概要

• エントリーDOI: 10.2210/pdb1zfl/pdb
• 関連するPDBエントリー: 1DTD 1DTV 1ZFI
• 分子名称: Metallocarboxypeptidase inhibitor (1 entity in total)
• 機能のキーワード: carboxypeptidase inhibitor, folding intermediate, oxidative folding, four-stranded antiparallel beta-sheet, hydrolase inhibitor
• 由来する生物種: Hirudo medicinalis (medicinal leech)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 7397.26

構造登録者

Arolas, J.L.,D'Silva, L.,Popowicz, G.M.,Aviles, F.X.,Holak, T.A.,Ventura, S. (登録日: 2005-04-20, 公開日: 2005-09-13, 最終更新日: 2024-11-20)

主引用文献

Arolas, J.L.,D'Silva, L.,Popowicz, G.M.,Aviles, F.X.,Holak, T.A.,Ventura, S.
NMR structural characterization and computational predictions of the major intermediate in oxidative folding of leech carboxypeptidase inhibitor
STRUCTURE, 13:1193-1202, 2005

PubMed Abstract: The III-A intermediate constitutes the major rate-determining step in the oxidative folding of leech carboxypeptidase inhibitor (LCI). In this work, III-A has been directly purified from the folding reaction and structurally characterized by NMR spectroscopy. This species, containing three native disulfides, displays a highly native-like structure; however, it lacks some secondary structure elements, making it more flexible than native LCI. III-A represents a structurally determined example of a disulfide-insecure intermediate; direct oxidation of this species to the fully native protein seems to be restricted by the burial of its two free cysteine residues inside a native-like structure. We also show that theoretical approaches based on topological constraints predict with good accuracy the presence of this folding intermediate. Overall, the derived results suggest that, as it occurs with non-disulfide bonded proteins, native-like interactions between segments of secondary structure rather than the crosslinking of disulfide bonds direct the folding of LCI.

PubMed: 16084391
DOI: 10.1016/j.str.2005.05.008

実験手法

SOLUTION NMR