Interfacial water as a "hydration fingerprint" in the noncognate complex of BamHI.

Abstract:

:The molecular code of specific DNA recognition by proteins as a paradigm in molecular biology remains an unsolved puzzle primarily because of the subtle interplay between direct protein-DNA interaction and the indirect contribution from water and ions. Transformation of the nonspecific, low affinity complex to a specific, high affinity complex is accompanied by the release of interfacial water molecules. To provide insight into the conversion from the loose to the tight form, we characterized the structure and energetics of water at the protein-DNA interface of the BamHI complex with a noncognate sequence and in the specific complex. The fully hydrated models were produced with Grand Canonical Monte Carlo simulations. Proximity analysis shows that water distributions exhibit sequence dependent variations in both complexes and, in particular, in the noncognate complex they discriminate between the correct and the star site. Variations in water distributions control the number of water molecules released from a given sequence upon transformation from the loose to the tight complex as well as the local entropy contribution to the binding free energy. We propose that interfacial waters can serve as a "hydration fingerprint" of a given DNA sequence.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Fuxreiter M,Mezei M,Simon I,Osman R

doi

10.1529/biophysj.105.063263

subject

Has Abstract

pub_date

2005-08-01 00:00:00

pages

903-11

issue

2

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(05)72742-9

journal_volume

89

pub_type

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