3pfu | pdb_00003pfu

N-terminal domain of Thiol:disulfide interchange protein DsbD in its reduced form

spinqualitylabelsall models 3pfu, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3pfu is a 1 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: DTT Related: 1l6p, 1jpe, 1vrs Gene: dsbD, cutA2, cycZ, dipZ, b4136, JW5734 (ECOLI) Activity: Protein-disulfide reductase, with EC number 1.8.1.8 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [DSBD_ECOLI] Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm, thereby maintaining the active site of DsbC, DsbE and DsbG in a reduced state. This transfer involves a cascade of disulfide bond formation and reduction steps.[HAMAP-Rule:MF_00399] Publication Abstract from PubMed Bacterial growth and pathogenicity depend on the correct formation of disulfide bonds, a process controlled by the Dsb system in the periplasm of Gram-negative bacteria. Proteins with a thioredoxin fold play a central role in this process. A general feature of thiol-disulfide exchange reactions is the need to avoid a long lived product complex between protein partners. We use a multidisciplinary approach, involving NMR, x-ray crystallography, surface plasmon resonance, mutagenesis, and in vivo experiments, to investigate the interaction between the two soluble domains of the transmembrane reductant conductor DsbD. Our results show oxidation state-dependent affinities between these two domains. These observations have implications for the interactions of the ubiquitous thioredoxin-like proteins with their substrates, provide insight into the key role played by a unique redox partner with an immunoglobulin fold, and are of general importance for oxidative protein-folding pathways in all organisms. Oxidation state-dependent protein-protein interactions in disulfide cascades.,Mavridou DA, Saridakis E, Kritsiligkou P, Goddard AD, Stevens JM, Ferguson SJ, Redfield C J Biol Chem. 2011 Jul 15;286(28):24943-56. Epub 2011 May 3. PMID:21543317 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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