1KNG

Crystal structure of CcmG reducing oxidoreductase at 1.14 A

Summary for 1KNG

• Entry DOI: 10.2210/pdb1kng/pdb
• Descriptor: THIOL:DISULFIDE INTERCHANGE PROTEIN CYCY (2 entities in total)
• Functional Keywords: thioredoxin fold, cytochrome c maturation, atomic resolution, oxidoreductase
• Biological source: Bradyrhizobium japonicum
• Cellular location: Periplasm (Probable): P30960
• Total number of polymer chains: 1
• Total formula weight: 16893.37

Authors

Edeling, M.A.,Guddat, L.W.,Fabianek, R.A.,Thony-Meyer, L.,Martin, J.L. (deposition date: 2001-12-18, release date: 2002-07-17, Last modification date: 2024-10-30)

Primary citation

Edeling, M.A.,Guddat, L.W.,Fabianek, R.A.,Thony-Meyer, L.,Martin, J.L.
Structure of CcmG/DsbE at 1.14 A resolution: high-fidelity reducing activity in an indiscriminately oxidizing environment
Structure, 10:973-979, 2002

PubMed 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 binding scaffold, the TRX fold, into a highly specific redox protein.

PubMed: 12121652
DOI: 10.1016/S0969-2126(02)00794-3

Experimental method

X-RAY DIFFRACTION (1.14 Å)