PcrH: Difference between revisions

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<StructureSection load='2xcb' size='340' side='right' caption='PcrH (grey, green) complex with PopD chaperone binding peptide (pink) and NO3- ion (PDB code [[2xcb]])' scene=''>
<StructureSection load='2xcb' size='350' side='right' caption='PcrH (magenta, green) complex with PopD chaperone binding peptide (cyan) and NO3- ion (PDB code [[2xcb]])' scene='72/725368/Cv/1'>


== Function ==
== Function ==

Revision as of 15:51, 15 February 2016


Function

PcrH 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 highlights

PcrH contains a helical Tpr domain (tetratricopeptide) which interacts with the translocator PopD or PopB peptide[1]. PopD peptide binds at the concave surface of PcrH.


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

Drag the structure with the mouse to rotate

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

  1. 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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman