1eej: Difference between revisions

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-{{Seed}}
-[[Image:1eej.png|left|200px]]
-<!--
+==CRYSTAL STRUCTURE OF THE PROTEIN DISULFIDE BOND ISOMERASE, DSBC, FROM ESCHERICHIA COLI==
-The line below this paragraph, containing "STRUCTURE_1eej", creates the "Structure Box" on the page.
+<StructureSection load='1eej' size='340' side='right'caption='[[1eej]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1eej]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EEJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EEJ FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr>
-{{STRUCTURE_1eej|  PDB=1eej  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1eej FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eej OCA], [https://pdbe.org/1eej PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eej RCSB], [https://www.ebi.ac.uk/pdbsum/1eej PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eej ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/DSBC_ECOLI DSBC_ECOLI] Acts as a disulfide isomerase, interacting with incorrectly folded proteins to correct non-native disulfide bonds. DsbG and DsbC are part of a periplasmic reducing system that controls the level of cysteine sulfenylation, and provides reducing equivalents to rescue oxidatively damaged secreted proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbC is reoxidized by DsbD.<ref>PMID:19965429</ref>
+== 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/ee/1eej_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=1eej ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-===CRYSTAL STRUCTURE OF THE PROTEIN DISULFIDE BOND ISOMERASE, DSBC, FROM ESCHERICHIA COLI===
+Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli.,McCarthy AA, Haebel PW, Torronen A, Rybin V, Baker EN, Metcalf P Nat Struct Biol. 2000 Mar;7(3):196-9. PMID:10700276<ref>PMID:10700276</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1eej" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_10700276}}, adds the Publication Abstract to the page
+*[[Thiol:disulfide interchange protein|Thiol:disulfide interchange protein]]
-(as it appears on PubMed at http://www.pubmed.gov), where 10700276 is the PubMed ID number.
+*[[Thiol:disulfide interchange protein 3D structures|Thiol:disulfide interchange protein 3D structures]]
--->
+== References ==
-{{ABSTRACT_PUBMED_10700276}}
+<references/>
+__TOC__
-==About this Structure==
+</StructureSection>
-EEJ is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EEJ OCA].
-==Reference==
-<ref group="xtra">PMID:10700276</ref><references group="xtra"/>
 [[Category: Escherichia coli]]
-[[Category: Protein disulfide-isomerase]]
+[[Category: Large Structures]]
-[[Category: Baker, E N.]]
+[[Category: Baker EN]]
-[[Category: Haebel, P W.]]
+[[Category: Haebel PW]]
-[[Category: McCarthy, A A.]]
+[[Category: McCarthy AA]]
-[[Category: Metcalf, P.]]
+[[Category: Metcalf P]]
-[[Category: Rybin, V.]]
+[[Category: Rybin V]]
-[[Category: Torronen, A.]]
+[[Category: Torronen A]]
-[[Category: Oxidoreductase]]
-[[Category: Protein disulfide isomerase]]
-[[Category: Protein folding]]
-[[Category: Redox protein]]
-[[Category: Redox-active center]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 02:04:58 2009''