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
Biochemistryjournal_title
Biochemistryauthors
le Coutre J,Turk E,Kaback HR,Wright EMdoi
10.1021/bi025692dsubject
Has Abstractpub_date
2002-06-25 00:00:00pages
8082-6issue
25eissn
0006-2960issn
1520-4995pii
bi025692djournal_volume
41pub_type
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