1kng: Difference between revisions

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[[Image:1kng.gif|left|200px]]
{{Seed}}
[[Image:1kng.png|left|200px]]


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{{STRUCTURE_1kng|  PDB=1kng  |  SCENE=  }}  
{{STRUCTURE_1kng|  PDB=1kng  |  SCENE=  }}  


'''Crystal structure of CcmG reducing oxidoreductase at 1.14 A'''
===Crystal structure of CcmG reducing oxidoreductase at 1.14 A===




==Overview==
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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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{{ABSTRACT_PUBMED_12121652}}


==About this Structure==
==About this Structure==
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[[Category: Cytochrome c maturation]]
[[Category: Cytochrome c maturation]]
[[Category: Thioredoxin fold]]
[[Category: Thioredoxin fold]]
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