Active water in protein-protein communication within the membrane: the case of SRII-HtrII signal relay.

Abstract:

:We detect internal water molecules in a membrane-embedded receptor-transducer complex and demonstrate water structure changes during formation of the signaling state. Time-resolved FTIR spectroscopy reveals stimulus-induced repositioning of one or more structurally active water molecules to a significantly more hydrophobic environment in the signaling state of the sensory rhodopsin II (SRII)-transducer (HtrII) complex. These waters, distinct from bound water molecules within the SRII receptor, appear to be in the middle of the transmembrane interface region near the Tyr199(SRII)-Asn74(HtrII) hydrogen bond. We conclude that water potentially plays an important role in the SRII --> HtrII signal transfer mechanism in the membrane's hydrophobic core.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Bergo VB,Spudich EN,Spudich JL,Rothschild KJ

doi

10.1021/bi802180a

subject

Has Abstract

pub_date

2009-02-10 00:00:00

pages

811-3

issue

5

eissn

0006-2960

issn

1520-4995

pii

10.1021/bi802180a

journal_volume

48

pub_type

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