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  • Structure of CcmG/DsbE at 1.14 Å resolution: High-fidelity reducing activity in an indiscriminately oxidizing environment

    Author(s)
    Edeling, MA
    Guddat, LW
    Fabianek, RA
    Thony-Meyer, L
    Martin, JL
    Griffith University Author(s)
    Martin, Jennifer
    Year published
    2002
    Metadata
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    Abstract
    CcmG is unlike other periplasmic thioredoxin (TRX)-like proteins in that it has a specific reducing activity in an oxidizing environment and a high fidelity of interaction. These two unusual properties are required for its role in c-type cytochrome maturation. The crystal structure of CcmG reveals a modified TRX fold with an unusually acidic active site and a groove formed from two inserts in the fold. Deletion of one of the groove-forming inserts disrupts c-type cytochrome formation. Two unique structural features of CcmG—an acidic active site and an adjacent groove—appear to be necessary to convert an indiscriminately ...
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    CcmG is unlike other periplasmic thioredoxin (TRX)-like proteins in that it has a specific reducing activity in an oxidizing environment and a high fidelity of interaction. These two unusual properties are required for its role in c-type cytochrome maturation. The crystal structure of CcmG reveals a modified TRX fold with an unusually acidic active site and a groove formed from two inserts in the fold. Deletion of one of the groove-forming inserts disrupts c-type cytochrome formation. Two unique structural features of CcmG—an acidic active site and an adjacent groove—appear to be necessary to convert an indiscriminately binding scaffold, the TRX fold, into a highly specific redox protein.
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    Journal Title
    Structure
    Volume
    10
    Issue
    7
    DOI
    https://doi.org/10.1016/S0969-2126(02)00794-3
    Subject
    Chemical sciences
    Biological sciences
    Biochemistry and cell biology not elsewhere classified
    Information and computing sciences
    Publication URI
    http://hdl.handle.net/10072/347889
    Collection
    • Journal articles

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