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1kng
From Proteopedia
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==Crystal structure of CcmG reducing oxidoreductase at 1.14 A== | ==Crystal structure of CcmG reducing oxidoreductase at 1.14 A== | ||
| - | <StructureSection load='1kng' size='340' side='right' caption='[[1kng]], [[Resolution|resolution]] 1.14Å' scene=''> | + | <StructureSection load='1kng' size='340' side='right'caption='[[1kng]], [[Resolution|resolution]] 1.14Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1kng]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1kng]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KNG FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.14Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kng OCA], [https://pdbe.org/1kng PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kng RCSB], [https://www.ebi.ac.uk/pdbsum/1kng PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kng ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/CYCY_BRADU CYCY_BRADU] Required for disulfide bond formation in some periplasmic proteins. Also acts as a disulfide oxidoreductase in cytochromes c biogenesis. The cysteines of apocytochromes c must be in the reduced state for covalent linkage between the two moieties to occur (By similarity). |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kn/1kng_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kn/1kng_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
| - | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1kng ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | 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. | ||
| - | |||
| - | 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<ref>PMID:12121652</ref> | ||
| - | + | ==See Also== | |
| - | + | *[[Thiol:disulfide interchange protein 3D structures|Thiol:disulfide interchange protein 3D structures]] | |
| - | == | + | |
| - | + | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bradyrhizobium japonicum]] | [[Category: Bradyrhizobium japonicum]] | ||
| - | [[Category: Edeling | + | [[Category: Large Structures]] |
| - | [[Category: Fabianek | + | [[Category: Edeling MA]] |
| - | [[Category: Guddat | + | [[Category: Fabianek RA]] |
| - | [[Category: Martin | + | [[Category: Guddat LW]] |
| - | [[Category: Thony-Meyer | + | [[Category: Martin JL]] |
| - | + | [[Category: Thony-Meyer L]] | |
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Current revision
Crystal structure of CcmG reducing oxidoreductase at 1.14 A
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