The crystal structure of the mycobacterial trehalose monomycolate transport factor A, TtfA, reveals an atypical fold
Ung KL, Alsarraf HMAB, Kremer L, Blaise M
Proteins · 2019-12
Abstract
Trehalose monomycolate (TMM) represents an essential element of the mycobacterial envelope. While synthesized in the cytoplasm, TMM is transported across the inner membrane by MmpL3 but, little is known regarding the MmpL3 partners involved in this process. Recently, the TMM transport factor A (TtfA) was found to form a complex with MmpL3 and to participate in TMM transport, although its biological role remains to be established. Herein, we report the crystal structure of the Mycobacterium smegmatis TtfA core domain. The phylogenetic distribution of TtfA homologues in non-mycolate containing bacteria suggests that TtfA may exert additional functions.
MeSH terms
- Cell Wall
- Escherichia coli
- Mycobacterium smegmatis
- Mycobacterium tuberculosis
- Cord Factors
- Bacterial Proteins
- Membrane Transport Proteins
- Recombinant Proteins
- Crystallography, X-Ray
- Cloning, Molecular
- Sequence Alignment
- Phylogeny
- Gene Expression
- Binding Sites
- Amino Acid Sequence
- Protein Binding
- Protein Folding
- Sequence Homology, Amino Acid
- Biological Transport
- Genetic Vectors
- Models, Molecular
- Protein Interaction Domains and Motifs
- Protein Conformation, alpha-Helical
- Protein Conformation, beta-Strand