The solution structure of ChaB, a putative membrane ion antiporter regulator from Escherichia coli

Osborne, Michael J.; Siddiqui, Nadeem; Iannuzzi, Pietro; Gehring, Kalle
January 2004
BMC Structural Biology;2004, Vol. 4, p1
Academic Journal
Background: ChaB is a putative regulator of ChaA, a Na+/H+ antiporter that also has Ca+/H+ activity in E. coli. ChaB contains a conserved 60-residue region of unknown function found in other bacteria, archaeabacteria and a series of baculoviral proteins. As part of a structural genomics project, the structure of ChaB was elucidated by NMR spectroscopy. Results: The structure of ChaB is composed of 3 α-helices and a small sheet that pack tightly to form a fold that is found in the cyclin-box family of proteins. Conclusion: ChaB is distinguished from its putative DNA binding sequence homologues by a highly charged flexible loop region that has weak affinity to Mg2+ and Ca2+ divalent metal ions.


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