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1kng
From Proteopedia
(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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| - | [[Image:1kng.gif|left|200px]]<br /><applet load="1kng" size=" | + | [[Image:1kng.gif|left|200px]]<br /><applet load="1kng" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1kng, resolution 1.14Å" /> | caption="1kng, resolution 1.14Å" /> | ||
'''Crystal structure of CcmG reducing oxidoreductase at 1.14 A'''<br /> | '''Crystal structure of CcmG reducing oxidoreductase at 1.14 A'''<br /> | ||
==Overview== | ==Overview== | ||
| - | CcmG is unlike other periplasmic thioredoxin (TRX)-like proteins in that | + | 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== | ==About this Structure== | ||
| - | 1KNG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bradyrhizobium_japonicum Bradyrhizobium japonicum]. Full crystallographic information is available from [http:// | + | 1KNG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bradyrhizobium_japonicum Bradyrhizobium japonicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KNG OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bradyrhizobium japonicum]] | [[Category: Bradyrhizobium japonicum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Edeling, M | + | [[Category: Edeling, M A.]] |
| - | [[Category: Fabianek, R | + | [[Category: Fabianek, R A.]] |
| - | [[Category: Guddat, L | + | [[Category: Guddat, L W.]] |
| - | [[Category: Martin, J | + | [[Category: Martin, J L.]] |
[[Category: Thony-Meyer, L.]] | [[Category: Thony-Meyer, L.]] | ||
[[Category: atomic resolution]] | [[Category: atomic resolution]] | ||
| Line 22: | Line 22: | ||
[[Category: thioredoxin fold]] | [[Category: thioredoxin fold]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:35:59 2008'' |
Revision as of 11:36, 21 February 2008
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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 Thu Feb 21 13:35:59 2008
