3e9j
From Proteopedia
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- | [[ | + | ==Structure of the charge-transfer intermediate of the transmembrane redox catalyst DsbB== |
+ | <StructureSection load='3e9j' size='340' side='right' caption='[[3e9j]], [[Resolution|resolution]] 3.70Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[3e9j]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E9J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3E9J FirstGlance]. <br> | ||
+ | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=UQ1:UBIQUINONE-1'>UQ1</scene><br> | ||
+ | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dsbA, dsf, ppfA, b3860, JW3832 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 Escherichia coli K-12]), dsbB, roxB, ycgA, b1185, JW5182 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 Escherichia coli K-12])</td></tr> | ||
+ | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3e9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e9j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3e9j RCSB], [http://www.ebi.ac.uk/pdbsum/3e9j PDBsum]</span></td></tr> | ||
+ | <table> | ||
+ | == 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/e9/3e9j_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Disulfide bond formation is a critical step in the folding of many secretory proteins. In bacteria, disulfide bonds are introduced by the periplasmic dithiol oxidase DsbA, which transfers its catalytic disulfide bond to folding polypeptides. Reduced DsbA is reoxidized by ubiquinone Q8, catalyzed by inner membrane quinone reductase DsbB. Here, we report the preparation of a kinetically stable ternary complex between wild-type DsbB, containing all essential cysteines, Q8 and DsbA covalently bound to DsbB. The crystal structure of this trapped DsbB reaction intermediate exhibits a charge-transfer interaction between Q8 and the Cys44 in the DsbB reaction center providing experimental evidence for the mechanism of de novo disulfide bond generation in DsbB. | ||
- | + | Preparation and structure of the charge-transfer intermediate of the transmembrane redox catalyst DsbB.,Malojcic G, Owen RL, Grimshaw JP, Glockshuber R FEBS Lett. 2008 Oct 15;582(23-24):3301-7. Epub 2008 Sep 5. PMID:18775700<ref>PMID:18775700</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
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==See Also== | ==See Also== | ||
*[[Protein disulfide oxidoreductase|Protein disulfide oxidoreductase]] | *[[Protein disulfide oxidoreductase|Protein disulfide oxidoreductase]] | ||
- | + | == References == | |
- | == | + | <references/> |
- | < | + | __TOC__ |
+ | </StructureSection> | ||
[[Category: Escherichia coli k-12]] | [[Category: Escherichia coli k-12]] | ||
[[Category: Glockshuber, R.]] | [[Category: Glockshuber, R.]] |
Revision as of 12:07, 29 September 2014
Structure of the charge-transfer intermediate of the transmembrane redox catalyst DsbB
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Categories: Escherichia coli k-12 | Glockshuber, R. | Malojcic, G. | Owen, R L. | Cell inner membrane | Cell membrane | Chaperone | Charge transfer reaction intermediate | Electron transport | Four helix bundle | Mechanism of disulfide bond formation | Membrane | Membrane protein complex | Oxidative protein folding in escherichia coli periplasm | Oxidoreductase | Redox-active center | Transmembrane | Transport | X-ray crystal structure