Unknown

Dataset Information

0

The solution structure of ChaB, a putative membrane ion antiporter regulator from Escherichia coli.


ABSTRACT: 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.

SUBMITTER: Osborne MJ 

PROVIDER: S-EPMC514712 | biostudies-literature | 2004 Aug

REPOSITORIES: biostudies-literature

altmetric image

Publications

The solution structure of ChaB, a putative membrane ion antiporter regulator from Escherichia coli.

Osborne Michael J MJ   Siddiqui Nadeem N   Iannuzzi Pietro P   Gehring Kalle K  

BMC structural biology 20040811


<h4>Background</h4>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.<h4>Results</h4>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 th  ...[more]

Similar Datasets

| S-EPMC2253234 | biostudies-literature
| S-EPMC1112004 | biostudies-literature
| S-EPMC2594013 | biostudies-literature
| S-EPMC4156090 | biostudies-literature
| S-EPMC4498715 | biostudies-literature
| S-EPMC2254304 | biostudies-literature
| S-EPMC1370855 | biostudies-literature
| S-EPMC262112 | biostudies-literature
| S-EPMC1322268 | biostudies-literature
| S-EPMC3258883 | biostudies-literature