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J. Biol. Chem., Vol. 278, Issue 12, 10112-10118, March 21, 2003
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From the Institut für Biophysik, Johann Wolfgang
Goethe-Universität, Theodor-Stern-Kai 7, Haus 74, D-60590
Frankfurt am Main, Germany
Infrared spectroscopy has been used to map
substrate-protein interactions: the conformational changes of the
sarcoplasmic reticulum Ca2+-ATPase upon nucleotide
binding and ATPase phosphorylation were monitored using the substrate
ATP and ATP analogues (2'-deoxy-ATP, 3'-deoxy-ATP, and inosine
5'-triphosphate), which were modified at specific functional groups of
the substrate. Modifications to the 2'-OH, the 3'-OH, and the amino
group of adenine reduce the extent of binding-induced conformational
change of the ATPase, with particularly strong effects observed for the
latter two. This demonstrates the structural sensitivity of the
nucleotide-ATPase complex to individual interactions between
nucleotide and ATPase. All groups studied are important for binding and
interactions of a given ligand group with the ATPase depend on
interactions of other ligand groups.
Phosphorylation of the ATPase was observed for ITP and 2'-deoxy-ATP,
but not for 3'-deoxy-ATP. There is no direct link between the extent of
conformational change upon nucleotide binding and the rate of
phosphorylation showing that the full extent of the ATP-induced
conformational change is not mandatory for phosphorylation. As observed
for the nucleotide-ATPase complex, the conformation of the first
phosphorylated ATPase intermediate E1PCa2 also depends on
the nucleotide, indicating that ATPase states have a less uniform conformation than previously anticipated.
Mapping Interactions between the Ca2+-ATPase and Its
Substrate ATP with Infrared Spectroscopy*
*
This work was supported by Deutsche Forschungsgemeinschaft
Grant Ba1887/2-1.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of Biochemistry
and Biophysics, Arrhenius Laboratories for Natural Sciences, Stockholm
University, S-106 91 Stockholm, Sweden. Tel.: 46-8-16-2452; Fax:
46-8-15-5597; E-mail: Andreas.Barth@dbb.su.se.
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