1sg7
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Revision as of 00:14, 21 November 2007
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NMR solution structure of the putative cation transport regulator ChaB
Overview
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.
About this Structure
1SG7 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
The solution structure of ChaB, a putative membrane ion antiporter regulator from Escherichia coli., Osborne MJ, Siddiqui N, Iannuzzi P, Gehring K, BMC Struct Biol. 2004 Aug 11;4:9. PMID:15306028
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