PcrH: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
PcrH contains a helical Tpr domain (tetratricopeptide) which interacts with the translocator PopD or PopB peptide<ref>PMID:20385547</ref>. PopD peptide binds at the concave surface of PcrH. | <scene name='72/725368/Cv/3'>PcrH contains a helical Tpr domain (tetratricopeptide) which interacts with the translocator PopD</scene> or PopB peptide<ref>PMID:20385547</ref>. 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> | ||
</StructureSection> | </StructureSection> | ||
Revision as of 16:17, 15 February 2016
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. See details in Molecular Playground/Pcr H. Structural highlightsor PopB peptide[1]. PopD peptide binds at the concave surface of PcrH. (PDB code 2xcb). [2]
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3D Structures of lactoferrin3D Structures of lactoferrin
Updated on 15-February-2016
2xcc - PaPcrH – Pseudomonas aeruginosa
2xcb - PaPcrH + PopD chaperone-binding peptide
4jl0 - PaPcrH + PopB chaperone-binding peptide
ReferencesReferences
- ↑ 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
- ↑ 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