Solvent interaction of a Hsp70 chaperone substrate-binding domain investigated with water-NOE NMR experiments.

Abstract:

:The interaction of solvent of the substrate binding domain of the bacterial heat shock 70 chaperone protein DnaK was studied in its apo form and with bound hydrophobic substrate peptide, using refined nuclear magnetic resonance experiments. Distinct differences between the two states of the protein were observed. According to our data, the apo form interacts more extensively with solvent than the peptide-bound form. Significantly, the open hydrophobic substrate binding cleft of DnaK in the apo form is found to contain several molecules of water which are displaced by the binding of the hydrophobic substrate, the peptide NRLLLTG. The solvent in the hydrophobic cleft has a residence time longer than 400 ps. It is predicted that the displacement of this trapped water must contribute to the binding free energy of the natural hydrophobic substrates of this class of protein-folding chaperone proteins.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Cai S,Stevens SY,Budor AP,Zuiderweg ER

doi

10.1021/bi030097c

subject

Has Abstract

pub_date

2003-09-30 00:00:00

pages

11100-8

issue

38

eissn

0006-2960

issn

1520-4995

journal_volume

42

pub_type

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