Publication details

The structural principles underlying molybdenum insertase complex assembly

Authors

HASSAN Ahmed Adel Ibrahim Hassona IHLING Christian IACOBUCCI Claudio KASTRITIS Panagiotis L SINZ Andrea KRUSE Tobias

Year of publication 2023
Type Article in Periodical
Magazine / Source Protein Science
MU Faculty or unit

Central European Institute of Technology

Citation
Web https://onlinelibrary.wiley.com/doi/full/10.1002/pro.4753
Doi http://dx.doi.org/10.1002/pro.4753
Keywords biosynthesis complex; molybdenum cofactor; molybdenum insertase
Description Within the cell, the trace element molybdenum (Mo) is only biologically active when complexed either within the nitrogenase-specific FeMo cofactor or within the molybdenum cofactor (Moco). Moco consists of an organic part, called molybdopterin (MPT) and an inorganic part, that is, the Mo-center. The enzyme which catalyzes the Mo-center formation is the molybdenum insertase (Mo-insertase). Mo-insertases consist of two functional domains called G- and E-domain. The G-domain catalyzes the formation of adenylated MPT (MPT-AMP), which is the substrate for the E-domain, that catalyzes the actual molybdate insertion reaction. Though the functions of E- and G-domain have been elucidated to great structural and mechanistic detail, their combined function is poorly characterized. In this work, we describe a structural model of the eukaryotic Mo-insertase Cnx1 complex that was generated based on cross-linking mass spectrometry combined with computational modeling. We revealed Cnx1 to form an asymmetric hexameric complex which allows the E- and G-domain active sites to align in a catalytic productive orientation toward each other.

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