1kng

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{{STRUCTURE_1kng| PDB=1kng | SCENE= }}
{{STRUCTURE_1kng| PDB=1kng | SCENE= }}
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'''Crystal structure of CcmG reducing oxidoreductase at 1.14 A'''
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===Crystal structure of CcmG reducing oxidoreductase at 1.14 A===
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==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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(as it appears on PubMed at http://www.pubmed.gov), where 12121652 is the PubMed ID number.
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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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:35:52 2008''

Revision as of 07:35, 2 July 2008

Image:1kng.png

Template:STRUCTURE 1kng

Crystal structure of CcmG reducing oxidoreductase at 1.14 A

Template:ABSTRACT PUBMED 12121652

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

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