The solution structure of ChaB, a putative membrane ion antiporter regulator from Escherichia coli.
[No authors listed]
摘要
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 alpha-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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基因功能
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原始数据
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文献解读
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