1kng

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[[Image:1kng.png|left|200px]]
 
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==Crystal structure of CcmG reducing oxidoreductase at 1.14 A==
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The line below this paragraph, containing "STRUCTURE_1kng", creates the "Structure Box" on the page.
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<StructureSection load='1kng' size='340' side='right'caption='[[1kng]], [[Resolution|resolution]] 1.14&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.14&#8491;</td></tr>
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<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>
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{{STRUCTURE_1kng| PDB=1kng | SCENE= }}
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</table>
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== Function ==
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[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).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kn/1kng_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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===Crystal structure of CcmG reducing oxidoreductase at 1.14 A===
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1kng" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_12121652}}, adds the Publication Abstract to the page
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*[[Thiol:disulfide interchange protein 3D structures|Thiol:disulfide interchange protein 3D structures]]
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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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== References ==
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<references/>
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{{ABSTRACT_PUBMED_12121652}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[1kng]] is a 1 chain structure with 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].
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==Reference==
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<ref group="xtra">PMID:012121652</ref><references group="xtra"/>
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[[Category: Bradyrhizobium japonicum]]
[[Category: Bradyrhizobium japonicum]]
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[[Category: Edeling, M A.]]
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[[Category: Large Structures]]
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[[Category: Fabianek, R A.]]
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[[Category: Edeling MA]]
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[[Category: Guddat, L W.]]
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[[Category: Fabianek RA]]
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[[Category: Martin, J L.]]
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[[Category: Guddat LW]]
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[[Category: Thony-Meyer, L.]]
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[[Category: Martin JL]]
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[[Category: Atomic resolution]]
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[[Category: Thony-Meyer L]]
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[[Category: Cytochrome c maturation]]
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[[Category: Oxidoreductase]]
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[[Category: Thioredoxin fold]]
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Current revision

Crystal structure of CcmG reducing oxidoreductase at 1.14 A

PDB ID 1kng

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