1sg7
From Proteopedia
NMR solution structure of the putative cation transport regulator ChaB
Structural highlights
FunctionCHAB_ECO57 Might be a regulator of the sodium-potassium/proton antiporter ChaA.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedBACKGROUND: 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. 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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