1iwf
From Proteopedia
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. 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 Page seeded by OCA on Fri May 2 20:30:21 2008
