The A-type ATP synthase subunit K of Methanopyrus kandleri is deduced from its sequence to form a monomeric rotor comprising 13 hairpin domains

FEBS Letters
Juke S Lolkema, Egbert J Boekema

Abstract

The ntpK gene of the archaeon Methanopyrus kandleri encodes the equivalent of the c subunit of ATP synthase. The gene product contains 1021 residues and consists of 13 homologous domains, each one corresponding to a single helical hairpin. The amino acid sequence of the domains is highly conserved, ranging between 50 and 80% sequence identity. Each of the 13 domains contains a conserved Gln and Glu residue in the N- and C-terminal helix, respectively, both of which are believed to be involved in cation binding. The protein is likely to form the monomeric rotor of the ATP synthase that consists of 13 hairpin domains.

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Citations

Sep 23, 2010·Proceedings of the National Academy of Sciences of the United States of America·Stuart J Ferguson
Mar 15, 2008·Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences·Mayumi Nakanishi-Matsui, Masamitsu Futai
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Feb 2, 2010·Yakugaku zasshi : Journal of the Pharmaceutical Society of Japan·Masatomo Maeda
Jul 23, 2014·PloS One·Julie E M McGeoch, Malcolm W McGeoch
Aug 11, 2004·Proceedings of the National Academy of Sciences of the United States of America·Noriyo MitomeMasasuke Yoshida
Feb 2, 2013·Bioarchitecture·Alastair G StewartDaniela Stock
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Dec 29, 2004·Biochimica Et Biophysica Acta·Jan P Dekker, Egbert J Boekema
Oct 19, 2005·Advances in Protein Chemistry·Stephan Wilkens
Jun 11, 2008·Biochemistry·Thomas KrebstakiesGabriele Deckers-Hebestreit
Jan 5, 2005·Micron : the International Research and Review Journal for Microscopy·Stephan WilkensYesha Zheng

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