1kng: Difference between revisions

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|ACTIVITY=  
|ACTIVITY=  
|GENE= cycy ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=375 Bradyrhizobium japonicum])
|GENE= cycy ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=375 Bradyrhizobium japonicum])
|DOMAIN=
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kng OCA], [http://www.ebi.ac.uk/pdbsum/1kng PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kng RCSB]</span>
}}
}}


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[[Category: thioredoxin fold]]
[[Category: thioredoxin fold]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:19:44 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:50:58 2008''

Revision as of 18:50, 30 March 2008

File:1kng.gif


Drag the structure with the mouse to rotate
1kng, resolution 1.14Å
Gene: cycy (Bradyrhizobium japonicum)
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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

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