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Structural properties of metal-free apometallothioneins.

Abstract：

:The metalated forms of metallothionein are well studied (particularly Zn-MT, Cu-MT and Cd-MT), but almost nothing is known about the chemical and structural properties of apometallothioneins despite their importance in initial metalation and subsequent demetalation. Electrospray ionization mass spectrometry was used to provide a detailed view of the structural properties of the metal-free protein. Mass spectra of Zn(7)-MT and apo-MT at pH 7 exhibit the same charge state distribution, indicating that apo-MT is tightly folded like the metallated protein, whereas apo-MT at pH 3 exhibits a charge state spectrum associated with unfolding or denaturation. Benzoquinone was used to modify the cysteines in the β-MT (9 Bq), and α-MT (11 Bq) fragments, and the full βα-MT (20 Bq) protein. ESI-MS showed that the overall volume and, therefore, the extent of folding for the modified proteins is similar to that of Zn-MT. Molecular modeling using MM3-MD methods provided the volume of each modified protein. The volumes of the partially modified proteins follow the same trend as the charge states, showing that ESI-MS is an excellent method with which to follow small changes in protein folding as a function of applied chemical stress. The data suggest that the structure of apo-βα-MT is more organized than previously considered.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Summers KL,Mahrok AK,Dryden MD,Stillman MJ

doi

10.1016/j.bbrc.2012.07.141

subject

Has Abstract

pub_date

2012-08-24 00:00:00

pages

485-92

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(12)01455-6

journal_volume

425

pub_type

杂志文章

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