Structural difference in the H+,K+-ATPase between the E1 and E2 conformations. An attenuated total reflection infrared spectroscopy, UV circular dichroism and raman spectroscopy study.
Conformational changes taking place in the gastric H+,K+-ATPase when shifting from the K+-induced E2 form to the E1 form upon replacing K+ ions by Na+ were investigated by different spectroscopic approaches. No significant secondary-structure change or secondary-structure reorientation with respect to the membrane plane could be measured by attenuated total reflection Fourier transform infrared spectroscopy of oriented films. Circular dichroism and Raman spectra obtained on tubulovesicle suspensions indicated no significant secondary structure or tyrosine and tryptophan side-chain environment changes in tubulovesicle suspensions. The smallest observable structural changes are discussed in term of the number of amino-acid residues involved for each technique.
Raussens
V
V
Laboratoire de Chimie-Physique des Macromolécules aux Interfaces, CP 206/2, Université Libre de Bruxelles, Campus Plaine, Belgium.
Pézolet
M
M
Ruysschaert
J M
JM
Goormaghtigh
E
E
D000818:Animals; D017506:H(+)-K(+)-Exchanging ATPase / Q000737:chemistry*; D011487:Protein Conformation; D013057:Spectrum Analysis / Q000379:methods*; D013552:Swine
D017506:H(+)-K(+)-Exchanging ATPase