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)
Year published
2002
Metadata
Show full item recordAbstract
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 ...
View more >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.
View less >
View more >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.
View less >
Journal Title
Structure
Volume
10
Issue
7
Subject
Chemical sciences
Biological sciences
Biochemistry and cell biology not elsewhere classified
Information and computing sciences