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Figure 8
(a) Superposition of EcAIII (gray) and structural homologs, F. meningosepticum AGA (fAGA, pink) and human AGA (hAGA, green), with the counterparts of selected EcAIII residues shown as sticks: Arg207 (Arg180/234 in fAGA/hAGA), Asp210 (Asp183/237 in fAGA/hAGA) and Ser211 (Ser184/238 in fAGA/hAGA). Black arrows mark the type of point mutations in fAGA (in magenta) and hAGA (in green) that led to misprocessing or reduced processing of AGA precursors. The cyan patches and frames mark the EcAIII sites mutated in this work and the pink patch marks the nucleophilic Thr residue. (b) Structural requirements necessary to initiate the maturation of Ntn-amidohydrolases and classification of the RDM1 variants of EcAIII according to the cause of the lack of autoprocessing. Mutants marked in pink are not cleaved into subunits, while those marked in blue are mature but are unable to hydrolyze L-Asn.

Journal logoSTRUCTURAL
BIOLOGY
ISSN: 2059-7983
Volume 78| Part 7| July 2022| Pages 911-926
https://doi.org/10.1107/S2059798322005691
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