Structural study of HA3 subcomponent of Clostridium botulinum type C progenitor toxin
نویسندگان
چکیده
Introduction The Clostridium botulinum neurotoxin (NTX) exists as seven different serotypes, designated A through G. In all seven serotypes, NTX are high molecular weight proteins that act on cholinergic neuromuscular junctions to block transmitter release. In culture fluid or food, most NTXs exist as a large stable complex (progenitor toxin) in association with nontoxic components, such as NTNHA and/or several different HAs. In the type C toxin, two forms of progenitor toxin, the C16S toxin and C12S toxin, have been identified. The C16S toxin contains of one molecule of NTX, one NTNHA, and several HA subcomponents. The HA subcomponents are designated HA1 (33 kDa), HA2 (17 kDa), and HA3 (70 kDa). HA3 can be further proteolytically cleaved to form the HA3a (22-23 kDa) and HA3b (55 kDa) fragments. Here we determined the three-dimensional structure of the HA3aHA3b complex.
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Purification, crystallization and preliminary X-ray analysis of an HA17-HA70 (HA2-HA3) complex from Clostridium botulinum type C progenitor toxin.
The haemagglutinin (HA) complex of Clostridium botulinum type C toxin is composed of three types of subcomponents: HA33, HA17 and HA70 (also known as HA1, HA2 and HA3, respectively). Here, a 260 kDa HA17-HA70 complex was crystallized. His-tagged HA17 and maltose-binding-protein-tagged HA70 were expressed in Escherichia coli and their complex was affinity-purified using a combination of amylose ...
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