Crystals of SctV from different species reveal variable symmetry for the cytosolic domain of the type III secretion system export gate.

ABSTRACT: Type III secretion systems (T3SSs) are proteinaceous devices employed by Gram-negative bacteria to directly transport proteins into a host cell. Substrate recognition and secretion are strictly regulated by the export apparatus of the so-called injectisome. The export gate SctV engages chaperone-bound substrates of the T3SS in its nonameric cytoplasmic domain. Here, the purification and crystallization of the cytoplasmic domains of SctV from Photorhabdus luminescens (LscV_C) and Aeromonas hydrophila (AscV_C) are reported. Self-rotation functions revealed that LscV_C forms oligomers with either eightfold or ninefold symmetry in two different crystal forms. Similarly, AscV_C was found to exhibit tenfold rotational symmetry. These are the first instance

SUBMITTER: Gilzer D 

PROVIDER: S-EPMC9629515 | biostudies-literature | 2022 Nov

REPOSITORIES: biostudies-literature