6lhz | pdb_00006lhz

Structure of aerolysin-like protein (Bombina maxima)

spinqualitylabelsall models 6lhz, resolution 2.52Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6lhz is a 1 chain structure with sequence from Bombina maxima. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.52Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Endolysosomes are key players in cell physiology, including molecular exchange, immunity, and environmental adaptation. They are the molecular target of some pore-forming aerolysin-like proteins (ALPs) that are widely distributed in animals and plants and are functionally related to bacterial toxin aerolysins. betagamma-CAT is a complex of an ALP (BmALP1) and a trefoil factor (BmTFF3) in the firebelly toad (Bombina maxima). It is the first example for 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 betagamma-CAT subunits and elimination of its biological activity. Consistent with its behavior in vitro, BmALP3 sensed environmental oxygen tension in vivo, leading to modulation of betagamma-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 on an active ALP (BmALP1) in a redox-dependent manner, a property that differs from those of bacterial toxin aerolysins. A cellular endolysosome-modulating pore-forming protein from a toad is negatively regulated by its paralog under oxidizing conditions.,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 J Biol Chem. 2020 Jun 4. pii: RA120.013556. doi: 10.1074/jbc.RA120.013556. PMID:32499370 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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