Sandbox Reserved 1500

This Sandbox is Reserved from 06/12/2018, through 30/06/2019 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1480 through Sandbox Reserved 1543.

To get started: Click the edit this page tab at the top. Save the page after each step, then edit it again. Click the 3D button (when editing, above the wikitext box) to insert Jmol. show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page. Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc. More help: Help:Editing

spinqualitylabelsall models PDB ID 5hfg Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Structural highlightsStructural highlights

5hfg is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	5hfi
Descriptor:	Uncharacterized protein, cytosolic disulfide reductase DsbM
Functional Keywords:	5hfi|dsb, dsbm, disulfide reductase, thioredoxin superfamilly, oridoreductase
Biological source:	Pseudomonas aeruginosa PAO1
Total number of polymer chains:	1
Total molecular weight:	25,286.7 Da
Authors:	Jo. I., Ha, N.-C. (release date : 2016-10-26)
Experimental method:	X-Ray diffraction (1.823Å) Those informations are from PDBJ.
Global symmetry:	Asymmetric - C1
Global stoichiometry:	Monomer - A
Secondary structure:	Beta sheets Figure 1: 5HFG secondary structure. , alpha helix
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Primary structurePrimary structure

5hfg is a 1 chain structure of 238 amino acids.

Secondary structureSecondary structure

The structure of 5hfg mainly consists in alpha helix (12) , beta sheets (4), you can check the 3D view here.

It has 2 main domains, the lid domain and the thioredoxine domain (see the picture).

Tertiary structureTertiary structure

5hfg behaves as a monomer or a dimer in solution but it has a monomeric composition. 5hfg is one distinct polypeptide molecule.

NatureNature

5hfg is a disulfide reductase DsbM from Pseudomonas aeruginosa. The Dsb family of proteins is mainly used to oxidize and reduce cysteine residues of substrate proteins. Most enzymes from Dsb-family catalyze disulfide formation in periplasmic or secreted substrate proteins.

It has no bound ligands and no modified residues. Sequence domains: Thioredoxin-like superfamily DSBA-like thioredoxin domain

FunctionFunction

This protein has a disulfide oxidoreductase activity, it is implicated in the reduction of the cytoplasmicredox-sensor protein OxyR in Pseudomonas aeruginosa. It contains a CXXC motif which sequence is homologous to the Dsb-family proteins. The CXXC motif is the actif site of the protein for the catalysis of disulfide oxidoreduction, moreover, this site also caracterize the affinity with the substrate protein. 5hfg presents a CGWC sequence in its CXXC motif, in which the Trp16 residue facilitates some hydrophobic interactions between the lid domain and the thioredoxine domain.

According to biochemical studies, 5hfg have also an ability to reduce the disulfide of OxyR (Hydrogen peroxide-inducible genes activator) that is formed by H2O2. The following photo shows a proposed mechanism of the action of DsbM in which the oxidized OxyR and the reduced glutathione are transported to the glutathione binding site of DsbM.