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• W3208554069 abstract "Molybdenum (Mo) is a crucial component for the survival of most species due to its vital duty for Mo-dependent enzymes. In nature, Mo is not biologically active unless it is complexed with a distinctive scaffold referred to as molybdopterin (MPT) to form a Molybdenum cofactor (Moco). Molybdenum insertases (Mo-insertases) are crucial for the final step of Moco biosynthesis in a multistep pathway that is evolutionary conserved. These combine the functions of two domains, referred to as G- and E- domain. In eukaryotes, the two domains are fused together, however, in prokaryotes, they are separate entities. In Escherichia coli, these are annotated as MogA and MoeA, while both domains fused in Arabidopsis thaliana and Homo sapiens are referred to as Cnx1 and gephyrin, respectively. The synthesis of Moco relies on the complex formation of Mo-insertases in order to protect and exchange intermediates. Protein-protein interaction was shown previously in Arabidopsis thaliana as well as a long-standing hypothesis of a hexagonal formation in the post synapse in mammals. The structure of the complex nor the full-length proteins was not previously identified in any species. This work presents the structure of Mo-insertase complex for MoeA-MogA, the full-length Cnx1 as well as gephyrin using crosslinking mass spectrometry (XL-MS), negative staining electron microscopy (negative staining EM) and computational modelling. For MoeA-MogA complex, Native Mass Spectrometry was done, giving insight into the stoichiometry and size of the complex. XL-MS and computational modelling showed how MogA would interact with MoeA, which was confirmed by negative staining EM. For full-length proteins, including Cnx1 and gephyrin, a novel approach was established to purify the protein complexes with minimal degradation products. XL-MS and computational modelling of Cnx1 showed 88 cross-links which hinted towards the G-domain to bind in two different orientations on the E-domain. These results elucidate the oligomerization of a possible mesh to be formed or a higher-order structure. Using the XL-MS results, the Cnx1 linker was ab initio modelled, as well as a possible MPT synthase - Cnx1 complex. Additionally, in order to understand more about the metabolic exchange between domains, site-directed mutagenesis was done to highlight the essential residues involved in complex formation. Preliminary results of the direct interaction of Mo-insertases with Moco-dependent enzyme was shown using crosslinking. Finally, the interaction between E- and G- domain of the human gephyrin was prevailed using negative staining EM and modelling." @default.
• W3208554069 created "2021-11-08" @default.
• W3208554069 creator A5008682765 @default.
• W3208554069 date "2021-09-09" @default.
• W3208554069 modified "2023-09-27" @default.
• W3208554069 title "The structural principles underlying Mo-insertase functionality and protein complex assembly" @default.
• W3208554069 doi "https://doi.org/10.24355/dbbs.084-202109090941-0" @default.
• W3208554069 hasPublicationYear "2021" @default.
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