View source for 5c00


==MdbA protein, a thiol-disulfide oxidoreductase from Corynebacterium diphtheriae==
<StructureSection load='5c00' size='340' side='right'caption='[[5c00]], [[Resolution|resolution]] 1.77&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5c00]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Corynebacterium_diphtheriae_NCTC_13129 Corynebacterium diphtheriae NCTC 13129]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C00 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5C00 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.77&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5c00 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c00 OCA], [https://pdbe.org/5c00 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5c00 RCSB], [https://www.ebi.ac.uk/pdbsum/5c00 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5c00 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q6NFK7_CORDI Q6NFK7_CORDI] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Gram-positive pathogen Corynebacterium diphtheriae exports through the Sec apparatus many extracellular proteins that include the key virulence factors diphtheria toxin and the adhesive pili. How these proteins attain their native conformations after translocation as unfolded precursors remains elusive. The fact that the majority of these exported proteins contain multiple cysteine residues and that several membrane-bound oxidoreductases are encoded in the corynebacterial genome suggest the existence of an oxidative protein-folding pathway in this organism. Here, we show that the shaft pilin SpaA harbors a disulfide bond in vivo and alanine substitution of these cysteins abrogates SpaA polymerization and leads to the secretion of degraded SpaA peptides. We then identified a thiol-disulfide oxidoreductase (MdbA), whose structure exhibits a conserved a thioredoxin-like domain with a CPHC active site. Remarkably, deletion of mdbA results in a severe temperature-sensitive cell division phenotype. This mutant also fails to assemble pilus structures and is greatly defective in toxin production. Consistent with these defects, the DeltamdbA mutant is attenuated in a guinea pig model of diphtheritic toxemia. Given its diverse cellular functions in cell division, pilus assembly and toxin production, we propose that MdbA is a component of the general oxidative folding machine in C. diphtheriae.

A thiol-disulfide oxidoreductase of the Gram-positive pathogen Corynebacterium diphtheriae is essential for viability, pilus assembly, toxin production, and virulence.,Reardon-Robinson ME, Osipiuk J, Jooya N, Chang C, Joachimiak A, Das A, Ton-That H Mol Microbiol. 2015 Aug 21. doi: 10.1111/mmi.13172. PMID:26294390<ref>PMID:26294390</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5c00" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Corynebacterium diphtheriae NCTC 13129]]
[[Category: Large Structures]]
[[Category: JOACHIMIAK A]]
[[Category: OSIPIUK J]]
[[Category: REARDON-ROBINSON ME]]
[[Category: TON-THAT H]]