1kng
From Proteopedia
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'''Crystal structure of CcmG reducing oxidoreductase at 1.14 A''' | '''Crystal structure of CcmG reducing oxidoreductase at 1.14 A''' | ||
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[[Category: Martin, J L.]] | [[Category: Martin, J L.]] | ||
[[Category: Thony-Meyer, L.]] | [[Category: Thony-Meyer, L.]] | ||
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| - | [[Category: | + | [[Category: Cytochrome c maturation]] |
| - | [[Category: | + | [[Category: Thioredoxin fold]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:57:00 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 19:57, 2 May 2008
Crystal structure of CcmG reducing oxidoreductase at 1.14 A
Overview
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.
About this Structure
1KNG is a Single protein structure of sequence from Bradyrhizobium japonicum. Full crystallographic information is available from OCA.
Reference
Structure of CcmG/DsbE at 1.14 A resolution: high-fidelity reducing activity in an indiscriminately oxidizing environment., Edeling MA, Guddat LW, Fabianek RA, Thony-Meyer L, Martin JL, Structure. 2002 Jul;10(7):973-9. PMID:12121652 Page seeded by OCA on Fri May 2 22:57:00 2008
