3c7m

<StructureSection load='3c7m' size='340' side='right' caption='[[3c7m]], [[Resolution|resolution]] 1.55&Aring;' scene=''>

<table><tr><td colspan='2'>[[3c7m]] is a 2 chain structure with sequence 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=3C7M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3C7M FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3c7m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c7m OCA], [http://pdbe.org/3c7m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3c7m RCSB], [http://www.ebi.ac.uk/pdbsum/3c7m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3c7m ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/DSBL_ECOL6 DSBL_ECOL6]] Involved in disulfide-bond formation. Acts by transferring its disulfide bond to other proteins. Part of a redox system composed of DsbI and DsbL that mediates formation of an essential disulfide bond in AssT.<ref>PMID:18565543</ref>

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== Publication Abstract from PubMed ==

Disulfide bond formation in the Escherichia coli periplasm requires the transfer of electrons from substrate proteins to DsbA, which is recycled as an oxidant by the membrane protein DsbB. The highly virulent, uropathogenic E. coli strain CFT073 contains a second, homologous pair of proteins, DsbL and DsbI, which are encoded in a tri-cistronic operon together with a periplasmic, uropathogen-specific arylsulfate sulfotransferase (ASST). We show that DsbL and DsbI form a functional redox pair, and that ASST is a substrate of DsbL/DsbI in vivo. DsbL is the most reactive oxidizing thioredoxin-like protein known to date. In contrast to DsbA, however, DsbL oxidizes reduced RNaseA with a much lower rate and prevents unspecific aggregation of reduced insulin. The 1.55 A resolution crystal structure of reduced DsbL provides insight into the reduced state of thioredoxin-like dithiol oxidases at high resolution, and reveals an unusual cluster of basic residues stabilizing the thiolate anion of the nucleophilic active-site cysteine. We propose that the DsbL/DsbI pair of uropathogenic E. coli was acquired as an additional, specific redox couple that guarantees biological activity of ASST.

 

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[[Category: Escherichia coli]]

[[Category: Capitani, G]]

[[Category: Glockshuber, R]]

[[Category: Grutter, M G]]

[[Category: Stirnimann, C U]]

[[Category: Oxidoreductase]]

[[Category: Periplasm]]

[[Category: Redox protein]]

[[Category: Redox-active center]]