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- W4247757208 abstract "The E. coli inducible lysine decarboxylase LdcI is an important acid stress response enzyme, whereas the AAA+ ATPase RavA is involved in multiple stress response pathways. A complex between these two proteins is thought to counteract acid stress under starvation in E. coli . We solved the crystal structure of the RavA monomer and combined it with a negative stain EM reconstruction of the RavA‐ADP hexamer (El Bakkouri et al ., 2010). We also determined the crystal structure of the LdcI double pentamer (Kanjee et al ., 2011). While these structures provided important insights into the functions of these individual proteins, the design principles of the LdcI‐RavA complex appeared even more enigmatic because it was difficult to envision how a decamer can bind a hexamer. CryoEM analysis allowed us to fit together the pieces of the jigsaw and revealed that the LdcI‐RavA complex is a surprising macromolecular cage of the size of a ribosome formed by two LdcI decamers and five RavA hexamers (Malet et al ., 2014). We identified molecular determinants of this interaction and specific elements essential for complex formation, as well as conformational rearrangements associated with the pH‐dependent LdcI activation and with the RavA binding (Malet et al ., 2014; Kandiah et al ., 2016). Moreover, we uncovered differences between the LdcI and its close paralogue, the second E. coli lysine decarboxylase LdcC thought to play mainly a biosynthetic role, finally explaining why only the acid stress response enzyme is capable of binding RavA and forming the cage. Multiple sequence alignment coupled to a phylogenetic analysis reveals that certain enterobacteria exert evolutionary pressure on the lysine decarboxylase towards the cage‐like assembly with RavA, implying that this complex may have an important function under particular stress conditions (Kandiah et al ., 2016). Research on structure‐functional relationships of this system by a combination of cryoEM, super‐resolution fluorescence microscopy and other structural, biochemical, biophysical and cell biology techniques is on‐going." @default.
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- W4247757208 date "2016-12-20" @default.
- W4247757208 modified "2023-10-18" @default.
- W4247757208 title "A huge but elusive macromolecular cage in enterobacterial stress response as seen by cryoEM and X-ray crystallography" @default.
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- W4247757208 doi "https://doi.org/10.1002/9783527808465.emc2016.8391" @default.
- W4247757208 hasPublicationYear "2016" @default.
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