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We previously determined the crystal structures of 1-Cys type selenoprotein MsrA from  Clostridium oremlandii  ( Co MsrA). The overall structure of  Co MsrA is unusual, consisting of two domains, the N-terminal catalytic domain and the C-terminal distinct helical domain which is absent from other known MsrA structures. Deletion of the helical domain almost completely abolishes the catalytic activity of  Co MsrA. In this study, we determined the crystal structure of the helical domain-deleted (ΔH-domain) form of  Co MsrA at a resolution of 1.76 Å. The monomer structure is composed of the central rolled mixed β-sheet surrounded by α-helices. However, there are significant conformational changes in the N- and C-termini and loop regions of the ΔH-domain protein relative to the catalytic domain structure of full-length  Co MsrA. The active site structure in the ΔH-domain protein completely collapses, thereby causing loss of catalytic activity of the protein. Interestingly, dimer structures are observed in the crystal formed by N-terminus swapping between two molecules. The ΔH-domain protein primarily exists as a dimer in solution, whereas the full-length  Co MsrA exists as a monomer. Collectively, this study provides insight into the structural basis of the essential role of the helical domain of  Co MsrA in its catalysis.

Essential Role of the C-Terminal Helical Domain in Active Site Formation of Selenoprotein MsrA from Clostridium oremlandii