The C‐terminal domain of Corynebacterium glutamicum mycoloyltransferase A is composed of five repeated motifs involved in cell wall binding and stability

What is it about?

The genomes of Mycobacteria and related species contain several genes encoding mycoloyltransferases that are specific cell envelope enzymes essential for the biogenesis of the outer membrane. We determined the crystal structure of the major mycoloyltransferase MytA of Corynebacterium glutamicum and found that its C-terminal domain forms a stalk composed of five repeated LGFP motifs (4-stranded -fold ) that interact specifically with the cell wall peptidoglycan-arabinogalactan polymer and contribute to the overall stability of the cell envelope.

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