PcrH

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Current revision (12:36, 29 July 2019) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
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<scene name='72/725368/Cv/3'>PcrH contains a helical Tpr domain (tetratricopeptide) which interacts with the translocator PopD</scene> or PopB peptide. PopD peptide binds at the concave surface of PcrH. <scene name='72/725368/Cv/5'>NO3- ion binding site</scene> (PDB code [[2xcb]]). <ref>PMID:20385547</ref>
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<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>

Current revision

PcrH (magenta, green) complex with PopD chaperone binding peptide (cyan) and NO3- ion (PDB code 2xcb)

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3D Structures of PcrH

Updated on 29-July-2019

2xcc - PaPcrH – Pseudomonas aeruginosa
2xcb - PaPcrH + PopD chaperone-binding peptide
4jl0 - PaPcrH + PopB chaperone-binding peptide

References

  1. 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
  2. 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

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Michal Harel, Joel L. Sussman, Alexander Berchansky

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