1kng

<table><tr><td colspan='2'>[[1kng]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"rhizobacterium_japonicum"_kirchner_1896 "rhizobacterium japonicum" kirchner 1896]. 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 [http://proteopedia.org/fgij/fg.htm?mol=1KNG FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cycy ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=375 "Rhizobacterium japonicum" Kirchner 1896])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1kng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kng OCA], [http://pdbe.org/1kng PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kng RCSB], [http://www.ebi.ac.uk/pdbsum/1kng PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1kng ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/CYCY_BRAJA CYCY_BRAJA]] Required for disulfide bond formation in some periplasmic proteins. Also act 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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== 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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Rhizobacterium japonicum kirchner 1896]]

[[Category: Edeling, M A]]

[[Category: Fabianek, R A]]

[[Category: Guddat, L W]]

[[Category: Martin, J L]]

[[Category: Thony-Meyer, L]]

[[Category: Thioredoxin fold]]