X-Ray studies reveal lanthanide binding sites at the A/B 5 interface of E. coli heat labile enterotoxin

The crystal structure determination of heat labile enterotoxin (LT) bound to two different lanthanide ions, erbium and samarium, revealed two distinct ion binding sites in the interface of the A subunit and the B pentamer of the toxin. One of the interface sites is conserved in the very similar chol...

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Bibliographic Details
Published in:FEBS letters 1992-02, Vol.297 (1), p.179-182
Main Authors: Sixma, Titia K., Terwisscha van Scheitinga, Anke C., Kalk, Kor H., Zhou, Kangjing, Wartna, Ellen S., Hol, Wim G.J.
Format: Article
Language:English
Subjects:
Calcium
Cholera toxin
Heat labile enterotoxin
Lanthanide ion: Conformational change
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Summary:The crystal structure determination of heat labile enterotoxin (LT) bound to two different lanthanide ions, erbium and samarium, revealed two distinct ion binding sites in the interface of the A subunit and the B pentamer of the toxin. One of the interface sites is conserved in the very similar cholera toxin sequence. These sites may be potential calcium binding sites. Erbium and samarium binding causes a change in the structure of LT: a rotation of the A1 subunit of up to two degrees relative to the B pentamer.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(92)80355-K