Structural highlights
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 PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Osborne MJ, Siddiqui N, Iannuzzi P, Gehring K. The solution structure of ChaB, a putative membrane ion antiporter regulator from Escherichia coli. BMC Struct Biol. 2004 Aug 11;4:9. PMID:15306028 doi:10.1186/1472-6807-4-9
