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Figure 6 | BMC Microbiology

Figure 6

From: Cleavage of the moaX-encoded fused molybdopterin synthase from Mycobacterium tuberculosis is necessary for activity

Figure 6

The role of the Gly81-Gly82 residues in MoaX. The Gly81 and Gly82 residues in MoaX are required for functionality. Mass spectrometry analysis of MoaX cleavage products confirmed that proteolytic processing occurs between the Gly82-Ser83 motifs to yield two functional MPT-synthase subunits. Mutation of Gly81 abrogates processing, yielding a non-functional, uncleaved derivative of MoaX suggesting that this residue is important for recognition/binding of the protease. In contrast, the G82→A mutation does not affect cleavage but the resulting MoaD-like subunit is not functional due to the absence of the terminal glycine, which is required for activation of MoaD by MoeB. However, the MoaE subunit that results from cleavage of this mutant protein can combine with the Msm MoaD2 to reconstitute a functional enzyme.

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