Ligand-induced differences in secondary structure of the Vibrio parahaemolyticus Na+/galactose cotransporter.

Abstract:

:A detailed structural study of the prokaryotic sodium/galactose transporter (vSGLT) from Vibrio parahaemolyticus using attenuated total reflection Fourier transform infrared (ATR-FTIR) spectroscopy reveals stepwise increases in alpha-helicity upon binding of sodium and D-galactose. These increases in helicity correlate with decreases in beta-structural elements. The changes are accompanied by stepwise reductions in the degree of H/D exchange (HDX), suggesting reduced accessibility of water to the protein backbone. The data demonstrate discrete conformational changes from one intermediate to the next during the catalytic cycle of the protein and are interpreted in a model of the symport reaction mechanism.

journal_name

Biochemistry

journal_title

Biochemistry

authors

le Coutre J,Turk E,Kaback HR,Wright EM

doi

10.1021/bi025692d

subject

Has Abstract

pub_date

2002-06-25 00:00:00

pages

8082-6

issue

25

eissn

0006-2960

issn

1520-4995

pii

bi025692d

journal_volume

41

pub_type

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