1iwf
From Proteopedia
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Solution structure of the N-terminal domain of pig gastric H/K-ATPase
Overview
It has been well established that phosphorylation is an important reaction, for the regulation of protein functions. In the N-terminal domain of the, alpha-chain of pig gastric H(+)/K(+)-ATPase, reversible sequential, phosphorylation occurs at Tyr 10 and Tyr 7. In this study, we determined, the structure of the peptide involving the residues from Gly 2 to Gly 34, of pig gastric H(+)/K(+)-ATPase and investigated the tyrosine, phosphorylation-induced conformational change using CD and NMR, experiments. The solution structure showed that the N-terminal fragment, has a helical conformation, and the peptide adopted two alpha-helices in, 50% trifluoroethanol (TFE) solvent, suggesting that the peptide has a high, helical propensity under hydrophobic conditions. Furthermore, the CD and, NMR data suggested that the structure of the N-terminal fragment becomes, more disordered as a result of phosphorylation of Tyr 10. This, conformational change induced by the phosphorylation of Tyr 10 might be an, advantageous reaction for sequential phosphorylation and may be important, for regulating the function of H(+)/K(+)-ATPase.
About this Structure
1IWF is a Single protein structure of sequence from [1]. Active as Hydrogen/potassium-exchanging ATPase, with EC number 3.6.3.10 Full crystallographic information is available from OCA.
Reference
Structure determination and conformational change induced by tyrosine phosphorylation of the N-terminal domain of the alpha-chain of pig gastric H+/K+-ATPase., Fujitani N, Kanagawa M, Aizawa T, Ohkubo T, Kaya S, Demura M, Kawano K, Nishimura S, Taniguchi K, Nitta K, Biochem Biophys Res Commun. 2003 Jan 3;300(1):223-9. PMID:12480547
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