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Your search keyword '"Heat labile enterotoxin"' showing total 4 results
Start Over Descriptor "Heat labile enterotoxin" Topic calcium
4 results on '"Heat labile enterotoxin"'

1. X-RAY STUDIES REVEAL LANTHANIDE BINDING-SITES AT THE A/B5 INTERFACE OF ESCHERICHIA-COLI HEAT LABILE ENTEROTOXIN

Subjects
MECHANISM, ADENYLATE-CYCLASE, VIBRIO-CHOLERAE, LANTHANIDE ION, CONFORMATIONAL CHANGE, CHOLERA-TOXIN, ERRORS, CHOLERA TOXIN, CALCIUM, HEAT LABILE ENTEROTOXIN, ESCHERICHIA-COLI, SUBUNIT, CALCIUM-TRANSPORT, DETECTOR
Abstract

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 Al subunit of up to two degrees relative to the B pentamer.

Published
1992

2. X-RAY STUDIES REVEAL LANTHANIDE BINDING-SITES AT THE A/B5 INTERFACE OF ESCHERICHIA-COLI HEAT LABILE ENTEROTOXIN

Subjects
MECHANISM, ADENYLATE-CYCLASE, VIBRIO-CHOLERAE, LANTHANIDE ION, CONFORMATIONAL CHANGE, CHOLERA-TOXIN, ERRORS, CHOLERA TOXIN, CALCIUM, HEAT LABILE ENTEROTOXIN, ESCHERICHIA-COLI, SUBUNIT, CALCIUM-TRANSPORT, DETECTOR
Abstract

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 Al subunit of up to two degrees relative to the B pentamer.

Published
1992

3. X-RAY STUDIES REVEAL LANTHANIDE BINDING-SITES AT THE A/B5 INTERFACE OF ESCHERICHIA-COLI HEAT LABILE ENTEROTOXIN

Author

SIXMA, TK, VANSCHELTINGA, ACT, KALK, KH, WARTNA, ES, HOL, WGJ, Groningen Biomolecular Sciences and Biotechnology, and Stratingh Institute for Chemistry

Subjects
MECHANISM, ADENYLATE-CYCLASE, VIBRIO-CHOLERAE, LANTHANIDE ION, CONFORMATIONAL CHANGE, CHOLERA-TOXIN, ERRORS, CHOLERA TOXIN, CALCIUM, HEAT LABILE ENTEROTOXIN, ESCHERICHIA-COLI, SUBUNIT, CALCIUM-TRANSPORT, DETECTOR
Abstract

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 Al subunit of up to two degrees relative to the B pentamer.

Published
1992

4. X-Ray studies reveal lanthanide binding sites at the A/B5 interface of E. coli heat labile enterotoxin

Author

Wim G. J. Hol, Titia K. Sixma, Kor H. Kalk, Ellen S. Wartna, Anke C. Terwisscha van Scheitinga, Kangjing Zhou, and Groningen Biomolecular Sciences and Biotechnology

Subjects
Lanthanide, Protein Conformation, Pentamer, Bacterial Toxins, Biophysics, chemistry.chemical_element, Enterotoxin, Heat-labile enterotoxin, medicine.disease_cause, Biochemistry, Enterotoxins, Ion binding, X-Ray Diffraction, Structural Biology, Cations, Genetics, medicine, Heat labile enterotoxin, Binding site, Molecular Biology, Samarium, Binding Sites, Chemistry, Lanthanide ion: Conformational change, Escherichia coli Proteins, Cholera toxin, Cell Biology, Conformational change, Crystallography, Calcium, Lanthanide ion, Erbium
Abstract

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.

Published
1992

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