6LHZ
Structure of aerolysin-like protein (Bombina maxima)
Summary for 6LHZ
| Entry DOI | 10.2210/pdb6lhz/pdb |
| Descriptor | aerolysin-like protein (2 entities in total) |
| Functional Keywords | pore-forming, aerolysin, amphibian, secretion, toxin |
| Biological source | Bombina maxima |
| Total number of polymer chains | 1 |
| Total formula weight | 17500.66 |
| Authors | Bian, X.L.,Wang, Q.Q.,Li, X.,Teng, M.Q.,Zhang, Y. (deposition date: 2019-12-10, release date: 2020-06-10, Last modification date: 2023-11-22) |
| Primary citation | Wang, Q.,Bian, X.,Zeng, L.,Pan, F.,Liu, L.,Liang, J.,Wang, L.,Zhou, K.,Lee, W.,Xiang, Y.,Li, S.,Teng, M.,Li, X.,Guo, X.,Zhang, Y. A cellular endolysosome-modulating pore-forming protein from a toad is negatively regulated by its paralog under oxidizing conditions. J.Biol.Chem., 295:10293-10306, 2020 Cited by PubMed Abstract: Endolysosomes are key players in cell physiology, including molecular exchange, immunity, and environmental adaptation. They are the molecular targets of some pore-forming aerolysin-like proteins (ALPs) that are widely distributed in animals and plants and are functionally related to bacterial toxin aerolysins. βγ-CAT is a complex of an ALP (BmALP1) and a trefoil factor (BmTFF3) in the firebelly toad (). It is the first example of a secreted endogenous pore-forming protein that modulates the biochemical properties of endolysosomes by inducing pore formation in these intracellular vesicles. Here, using a large array of biochemical and cell biology methods, we report the identification of BmALP3, a paralog of BmALP1 that lacks membrane pore-forming capacity. We noted that both BmALP3 and BmALP1 contain a conserved cysteine in their C-terminal regions. BmALP3 was readily oxidized to a disulfide bond-linked homodimer, and this homodimer then oxidized BmALP1 via disulfide bond exchange, resulting in the dissociation of βγ-CAT subunits and the elimination of biological activity. Consistent with its behavior , BmALP3 sensed environmental oxygen tension , leading to modulation of βγ-CAT activity. Interestingly, we found that this C-terminal cysteine site is well conserved in numerous vertebrate ALPs. These findings uncover the existence of a regulatory ALP (BmALP3) that modulates the activity of an active ALP (BmALP1) in a redox-dependent manner, a property that differs from those of bacterial toxin aerolysins. PubMed: 32499370DOI: 10.1074/jbc.RA120.013556 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.52 Å) |
Structure validation
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