PcrH: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<scene name='72/725368/Cv/ | <scene name='72/725368/Cv/6'>PcrH contains a helical Tpr domain (tetratricopeptide) which interacts with the translocator PopD</scene> or PopB peptide. Water molecules are shown as red spheres. PopD peptide binds at the concave surface of PcrH. <scene name='72/725368/Cv/7'>NO3- ion binding site</scene> (PDB code [[2xcb]]). <ref>PMID:20385547</ref> | ||
</StructureSection> | </StructureSection> |
Latest revision as of 15:36, 29 July 2019
FunctionPcrH or Regulatory protein PcrH is a chaperone protein which is a member of the translocon system which enables bacteria to form a pore in the cell wall for the insertion of toxins into it[1]. See details in Molecular Playground/Pcr H. Structural highlightsor PopB peptide. Water molecules are shown as red spheres. PopD peptide binds at the concave surface of PcrH. (PDB code 2xcb). [2]
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3D Structures of PcrH3D Structures of PcrH
Updated on 29-July-2019
2xcc - PaPcrH – Pseudomonas aeruginosa
2xcb - PaPcrH + PopD chaperone-binding peptide
4jl0 - PaPcrH + PopB chaperone-binding peptide
ReferencesReferences
- ↑ Broms JE, Forslund AL, Forsberg A, Francis MS. PcrH of Pseudomonas aeruginosa is essential for secretion and assembly of the type III translocon. J Infect Dis. 2003 Dec 15;188(12):1909-21. Epub 2003 Dec 3. PMID:14673772 doi:http://dx.doi.org/10.1086/379898
- ↑ Job V, Mattei PJ, Lemaire D, Attree I, Dessen A. Structural basis of chaperone recognition of type III secretion system minor translocator proteins. J Biol Chem. 2010 Jul 23;285(30):23224-32. Epub 2010 Apr 12. PMID:20385547 doi:10.1074/jbc.M110.111278