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.
CITATION STYLE
Osborne, M. J., Siddiqui, N., Iannuzzi, P., & Gehring, K. (2004). The solution structure of ChaB, a putative membrane ion antiporter regulator from Escherichia coli. BMC Structural Biology, 4, 1–11. https://doi.org/10.1186/1472-6807-4-1
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