Sandbox Reserved 1500

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=== Secondary structure ===
=== Secondary structure ===
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The structure of 5hfg mainly consists in alpha helix (12) , beta sheets (4), you can check the [http://www.rcsb.org/pdb/explore/jmol.do?structureId=5HFG&bionumber=1&opt=3&jmolMode=HTML5 3D view here]. [[Image:Example1.png]] [[Image:Example2.png]]
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The structure of 5hfg mainly consists in alpha helix (12) , beta sheets (4), you can check the [http://www.rcsb.org/pdb/explore/jmol.do?structureId=5HFG&bionumber=1&opt=3&jmolMode=HTML5 3D view here]. [[Image:Exemple1.png]] [[Image:Exemple2.png]]

Revision as of 16:44, 11 January 2019

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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PDB ID 5hfg

Drag the structure with the mouse to rotate

Contents

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.
Secondary structure:
Figure 1: 5HFG 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). Image:Capture1.PNG

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
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