Structural highlights
Publication Abstract from PubMed
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.
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 Dec 12. doi: 10.1002/prot.25863. PMID:31833106[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ung KL, Alsarraf HMAB, Kremer L, Blaise M. The crystal structure of the mycobacterial trehalose monomycolate transport factor A, TtfA, reveals an atypical fold. Proteins. 2019 Dec 12. doi: 10.1002/prot.25863. PMID:31833106 doi:http://dx.doi.org/10.1002/prot.25863
