1kng
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(New page: 200px<br /><applet load="1kng" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kng, resolution 1.14Å" /> '''Crystal structure of...)
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Revision as of 17:17, 20 November 2007
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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 Tue Nov 20 19:24:59 2007
