PilZ domain

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PilZ
PDB 1ywu EBI.jpg
the solution NMR structure of the protein of unknown function vca0042 from vibrio cholerae o1
Identifiers
Symbol PilZ
Pfam PF07238
InterPro IPR009875

The PilZ protein family is named after the type IV pilus control protein first identified in Pseudomonas aeruginosa, expressed as part of the pil operon. It has a cytoplasmic location and is essential for type IV fimbrial, or pilus, biogenesis.[1] PilZ is a c-di-GMP binding domain and PilZ domain-containing proteins represent the best studied class of c-di-GMP effectors.[2] C-di-GMP, cyclic diguanosine monophosphate, the second messenger in cells, is widespread in and unique to the bacterial kingdom.[3] Elevated intracellular levels of c-di-GMP generally cause bacteria to change from a motile single-cell state to a sessile, adhesive surface-attached multicellular state called biofilm.[4][5]

Proteins which contain PilZ are known to interact with the flagellar switch-complex proteins FliG and FliM and this is mediated via the c-di-GMP-PliZ complex. This interaction results in a reduction of torque-generation and induces counterclockwise motor bias that slows the motor and induces counterclockwise rotation, inhibiting chemotaxis.[6]

Binding and mutagenesis studies of several PilZ domain proteins have shown that c-di-GMP binding depends on residues in RxxxR and D/NxSxxG sequence-motifs. The crystal structure, at 1.7 A, of a PilZ domain::c-di-GMP complex from Vibrio cholerae shows c-di-GMP contacting seven of nine strongly conserved residues. Binding of c-di-GMP causes a conformational switch whereby the C- and N-terminal domains are brought into close opposition forming a new allosteric interaction surface that spans these domains and the c-di-GMP at their interface.[7]

The PilZ domain is also implicated in the bacterial pathogenicity of the Lyme disease spirochaete, Borrelia burgdorferi, through its binding partner c-di-GMP.[8]

References[edit]

  1. ^ Alm RA, Bodero AJ, Free PD, Mattick JS (January 1996). "Identification of a novel gene, pilZ, essential for type 4 fimbrial biogenesis in Pseudomonas aeruginosa". J. Bacteriol. 178 (1): 46–53. PMC 177619Freely accessible. PMID 8550441. 
  2. ^ Ryjenkov, DA; Simm, R; Römling, U; Gomelsky, M (Oct 13, 2006). "The PilZ domain is a receptor for the second messenger c-di-GMP: the PilZ domain protein YcgR controls motility in enterobacteria.". The Journal of Biological Chemistry. 281 (41): 30310–4. PMID 16920715. doi:10.1074/jbc.C600179200. 
  3. ^ Amikam, D; Galperin, MY (Jan 1, 2006). "PilZ domain is part of the bacterial c-di-GMP binding protein.". Bioinformatics (Oxford, England). 22 (1): 3–6. PMID 16249258. doi:10.1093/bioinformatics/bti739. 
  4. ^ Mattick, JS (2002). "Type IV pili and twitching motility.". Annual Review of Microbiology. 56: 289–314. PMID 12142488. doi:10.1146/annurev.micro.56.012302.160938. 
  5. ^ Wolfe, AJ; Visick, KL (Jan 2008). "Get the message out: cyclic-Di-GMP regulates multiple levels of flagellum-based motility.". Journal of Bacteriology. 190 (2): 463–75. PMC 2223684Freely accessible. PMID 17993515. doi:10.1128/JB.01418-07. 
  6. ^ Paul, K; Nieto, V; Carlquist, WC; Blair, DF; Harshey, RM (Apr 9, 2010). "The c-di-GMP binding protein YcgR controls flagellar motor direction and speed to affect chemotaxis by a "backstop brake" mechanism.". Molecular Cell. 38 (1): 128–39. PMC 2929022Freely accessible. PMID 20346719. doi:10.1016/j.molcel.2010.03.001. 
  7. ^ Benach, J; Swaminathan, SS; Tamayo, R; Handelman, SK; Folta-Stogniew, E; Ramos, JE; Forouhar, F; Neely, H; Seetharaman, J; Camilli, A; Hunt, JF (Dec 12, 2007). "The structural basis of cyclic diguanylate signal transduction by PilZ domains.". The EMBO Journal. 26 (24): 5153–66. PMC 2140105Freely accessible. PMID 18034161. doi:10.1038/sj.emboj.7601918. 
  8. ^ Pitzer, JE; Sultan, SZ; Hayakawa, Y; Hobbs, G; Miller, MR; Motaleb, MA (May 2011). "Analysis of the Borrelia burgdorferi cyclic-di-GMP-binding protein PlzA reveals a role in motility and virulence.". Infection and immunity. 79 (5): 1815–25. PMC 3088147Freely accessible. PMID 21357718. doi:10.1128/IAI.00075-11. 

This article incorporates text from the public domain Pfam and InterPro IPR009875

Category:Protein domains