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-[[Image:1eej.jpg|left|200px]]
+{{Seed}}
+[[Image:1eej.png|left|200px]]
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 {{STRUCTURE_1eej|  PDB=1eej  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF THE PROTEIN DISULFIDE BOND ISOMERASE, DSBC, FROM ESCHERICHIA COLI'''
+===CRYSTAL STRUCTURE OF THE PROTEIN DISULFIDE BOND ISOMERASE, DSBC, FROM ESCHERICHIA COLI===
-==Overview==
+<!--
-DsbC is one of five Escherichia coli proteins required for disulfide bond formation and is thought to function as a disulfide bond isomerase during oxidative protein folding in the periplasm. DsbC is a 2 x 23 kDa homodimer and has both protein disulfide isomerase and chaperone activity. We report the 1.9 A resolution crystal structure of oxidized DsbC where both Cys-X-X-Cys active sites form disulfide bonds. The molecule consists of separate thioredoxin-like domains joined via hinged linker helices to an N-terminal dimerization domain. The hinges allow relative movement of the active sites, and a broad uncharged cleft between them may be involved in peptide binding and DsbC foldase activities.
+The line below this paragraph, {{ABSTRACT_PUBMED_10700276}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10700276 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10700276}}
 ==About this Structure==
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 [[Category: Redox protein]]
 [[Category: Redox-active center]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 14:59:54 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 00:34:24 2008''