1kng: Difference between revisions
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==Crystal structure of CcmG reducing oxidoreductase at 1.14 A== | |||
<StructureSection load='1kng' size='340' side='right'caption='[[1kng]], [[Resolution|resolution]] 1.14Å' scene=''> | |||
== Structural highlights == | |||
<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='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'>[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> | |||
== 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 == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<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/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</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/main_output.php?pdb_ID=1kng ConSurf]. | |||
<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> | |||
CcmG | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1kng" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
*[[Thiol:disulfide interchange protein 3D structures|Thiol:disulfide interchange protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bradyrhizobium japonicum]] | [[Category: Bradyrhizobium japonicum]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Edeling | [[Category: Edeling MA]] | ||
[[Category: Fabianek | [[Category: Fabianek RA]] | ||
[[Category: Guddat | [[Category: Guddat LW]] | ||
[[Category: Martin | [[Category: Martin JL]] | ||
[[Category: Thony-Meyer | [[Category: Thony-Meyer L]] | ||
Latest revision as of 06:54, 30 October 2024
Crystal structure of CcmG reducing oxidoreductase at 1.14 A
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