Sandbox Reserved 1500

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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.

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

Contents 1 Structural highlights 1.1 Primary structure 1.2 Secondary structure 1.3 Tertiary structure 2 Nature 3 Function 4 Relevance 5 References

Structural 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
Secondary structure:	Figure 1: 5HFG secondary structure.[1] ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Global Symmetry: Asymmetric - C1

Global Stoichiometry: Monomer - A

Its theoretical weight is 25.29 KDa

Primary structure

5hfg is a 1 chain structure of 238 amino acids. ^[2]

Secondary structure

The structure of 5hfg mainly consists in alpha helix (12) , beta sheets (4), you can check the 3D view here. Image:Exemple1.png Image:Exemple2.png

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

Tertiary structure

5hfg behaves as a monomer or a dimer in solution but it has a monomeric composition. 5hfg is one distinct polypeptide molecule. ^[3]

Nature

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. This protein contain 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. ^[4]

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

Function

This protein has a disulfide oxidoreductase activity, it is implicated in the reduction of the cytoplasmicredox-sensor protein OxyR in Pseudomonas aeruginosa.

Relevance

Click to see a sample scene created with SAT by Group, and to see a transparent representation of the protein.

References

1. ↑ PDB image
2. ↑ https://www.rcsb.org/structure/5HFG
3. ↑ https://www.ebi.ac.uk/pdbe/entry/pdb/5HFG
4. ↑ https://www.researchgate.net/publication/308186632_Crystal_structures_of_the_disulfide_reductase_DsbM_from_Pseudomonas_aeruginosa