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The crystal structure of the mycobacterial trehalose monomycolate transport factor A, TtfA, reveals an atypical fold
Author(s) -
Ung Kien Lam,
Alsarraf Husam M. A. B.,
Kremer Laurent,
Blaise Mickaël
Publication year - 2020
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.25863
Subject(s) - mycobacterium smegmatis , cytoplasm , bacteria , chemistry , mycobacterium , cell envelope , biology , biochemistry , mycobacterium tuberculosis , genetics , escherichia coli , gene , medicine , tuberculosis , pathology
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.