6T84

crystal structure of the mycobacterial trehalose monomycolate transport factor A, TtfA

Summary for 6T84

Entry DOI	10.2210/pdb6t84/pdb
Descriptor	Uncharacterized protein, SULFATE ION (3 entities in total)
Functional Keywords	trehalose monomycolate, mmpl3 accessory protein, lipid transport
Biological source	Mycolicibacterium smegmatis MC2 155
Total number of polymer chains	1
Total formula weight	21609.74
Authors	Blaise, M. (deposition date: 2019-10-24, release date: 2019-12-25, Last modification date: 2024-05-15)
Primary citation	Ung, K.L.,Alsarraf, H.M.A.B.,Kremer, L.,Blaise, M. The crystal structure of the mycobacterial trehalose monomycolate transport factor A, TtfA, reveals an atypical fold. Proteins, 88:809-815, 2020 Cited by PubMed 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. PubMed: 31833106 DOI: 10.1002/prot.25863 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.4 Å)

Structure validation