Structural highlights
Function
ELBP_ECOLX The biological activity of the toxin is produced by the A chain, which activates intracellular adenyl cyclase.
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
Biological toxicity of E. coli heat-labile enterotoxin and the closely related cholera toxin requires that the assembled toxin be activated by proteolytic cleavage of the A subunit and reduction of a disulfide bond internal to the A subunit. The structural role served by this reduction and cleavage is not known, however. We have crystallographically determined the structure of the E. coli heat-labile enterotoxin AB5 hexamer in which the A subunit has been cleaved by trypsin between residues 192 and 195. The toxin is thus partially activated, in that it has been cleaved but the disulfide bond has not been reduced. The structure of the A subunit in the cleaved toxin is substantially the same as that previously observed for the uncleaved AB5 structure, suggesting that although such cleavage is required for biological activity of the toxin it does not by itself cause a conformational change.
Structure of partially-activated E. coli heat-labile enterotoxin (LT) at 2.6 A resolution.,Merritt EA, Pronk SE, Sixma TK, Kalk KH, van Zanten BA, Hol WG FEBS Lett. 1994 Jan 3;337(1):88-92. PMID:8276119[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Merritt EA, Pronk SE, Sixma TK, Kalk KH, van Zanten BA, Hol WG. Structure of partially-activated E. coli heat-labile enterotoxin (LT) at 2.6 A resolution. FEBS Lett. 1994 Jan 3;337(1):88-92. PMID:8276119
