8pys
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Cryo-EM structure of the DyP peroxidase-loaded encapsulin nanocompartment from Mycobacterium tuberculosis with icosahedral symmetry imposed.
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Structural highlights
FunctionENCAP_MYCTU Shell component of a type 1 encapsulin nanocompartment in situ; its cargo protects against oxidative stress at low pH. In situ and in E.coli assembles into proteinaceous shells about 22 nm in diameter with 2.5 nm thick walls (PubMed:24855650, PubMed:34751132). Cargo proteins are targeted to the interior via their C-terminal extensions; empty intact shells can be isolated in E.coli in the absence of cargo protein. There are at least 4 possible cargo proteins, DyP (encoded in the same locus), FolB, BfrB and Rv1762c; DyP and Rv1762c have been identified in vivo (PubMed:24855650). Probably involved in protection against oxidative damage from the host immune response (Probable) (PubMed:34751132). A T-cell antigen found in bacterial culture cell filtrates, stimulates mouse immune response. Does not have detectable bacteriocin activity (PubMed:9596740).[1] [2] [3] [4] References
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