3c71

<StructureSection load='3c71' size='340' side='right' caption='[[3c71]], [[Resolution|resolution]] 1.90&Aring;' scene=''>

<table><tr><td colspan='2'>[[3c71]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C71 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3C71 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1st9|1st9]], [[1su9|1su9]]</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=3c71 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c71 OCA], [http://pdbe.org/3c71 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3c71 RCSB], [http://www.ebi.ac.uk/pdbsum/3c71 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3c71 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/RESA_BACSU RESA_BACSU]] Thiol-disulfide oxidoreductase which is required in disulfide reduction during c-type cytochrome synthesis. May accept reducing equivalents from CcdA, leading to breakage of disulfide bonds in apocytochrome c; following this reduction heme can be covalently attached. Does not play a role in sporulation.<ref>PMID:12637552</ref>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c7/3c71_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

The thiol-disulfide oxidoreductase ResA from Bacillus subtilis fulfils a reductive role in cytochrome c maturation. The pK(a) values for the CEPC (one-letter code) active-site cysteine residues of ResA are unusual for thioredoxin-like proteins in that they are both high (&gt;8) and within 0.5 unit of each other. To determine the contribution of the inter-cysteine dipeptide of ResA to its redox and acid-base properties, three variants (CPPC, CEHC and CPHC) were generated representing a stepwise conversion into the active-site sequence of the high-potential DsbA protein from Escherichia coli. The substitutions resulted in large decreases in the pK(a) values of both the active-site cysteine residues: in CPHC (DsbA-type) ResA, DeltapK(a) values of -2.5 were measured for both cysteine residues. Increases in midpoint reduction potentials were also observed, although these were comparatively small: CPHC (DsbA-type) ResA exhibited an increase of +40 mV compared with the wild-type protein. Unfolding studies revealed that, despite the observed differences in the properties of the reduced proteins, changes in stability were largely confined to the oxidized state. High-resolution structures of two of the variants (CEHC and CPHC ResA) in their reduced states were determined and are discussed in terms of the observed changes in properties. Finally, the in vivo functional properties of CEHC ResA are shown to be significantly affected compared with those of the wild-type protein.

Effects of substitutions in the CXXC active-site motif of the extracytoplasmic thioredoxin ResA.,Lewin A, Crow A, Hodson CT, Hederstedt L, Le Brun NE Biochem J. 2008 Aug 15;414(1):81-91. PMID:18422485<ref>PMID:18422485</ref>

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

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<div class="pdbe-citations 3c71" style="background-color:#fffaf0;"></div>

*[[Protein disulfide oxidoreductase|Protein disulfide oxidoreductase]]

[[Category: Crow, A]]

[[Category: Cytochrome c-type biogenesis]]

[[Category: Membrane]]

[[Category: Transmembrane]]