Premium
X‐Ray studies reveal lanthanide binding sites at the A/B 5 interface of E. coli heat labile enterotoxin
Author(s) -
Sixma Titia K.,
Terwisscha van Scheitinga Anke C.,
Kalk Kor H.,
Zhou Kangjing,
Wartna Ellen S.,
Hol Wim G.J.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80355-k
Subject(s) - pentamer , chemistry , samarium , binding site , lanthanide , enterotoxin , heat labile enterotoxin , crystallography , cholera toxin , ion , protein subunit , stereochemistry , inorganic chemistry , biochemistry , biology , escherichia coli , organic chemistry , microbiology and biotechnology , gene
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.