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PDBsum entry 1oos
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protein Protein-protein interface(s) links
Chaperone PDB id
1oos

 

 

 

 

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Contents
Protein chains
134 a.a.
23 a.a.
Theoretical model
PDB id:
1oos
Name: Chaperone
Title: Tetratricopeptide repeats in type iii secretion chaperones and regulators
Structure: Low calcium response locus protein h. Chain: a. Yopd protein. Chain: b
Source: Yersinia pseudotuberculosis. Bacteria. Bacteria
Authors: M.J.Pallen,M.S.Francis,K.Futterer
Key ref: M.J.Pallen et al. (2003). Tetratricopeptide-like repeats in type-III-secretion chaperones and regulators. Fems Microbiol Lett, 223, 53-60. PubMed id: 12799000 DOI: 10.1016/S0378-1097(03)00344-6
Date:
04-Mar-03     Release date:   15-Jul-03    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P23995  (LCRH_YERPS) -  Low calcium response locus protein H
Seq:
Struc: 		168 a.a.
134 a.a.
Protein chain
Pfam   ArchSchema ?
Q06131  (YOPD_YERPS) -  Protein YopD
Seq:
Struc: 		306 a.a.
23 a.a.
Key:    PfamA domain  Secondary structure

 

 
DOI no: 10.1016/S0378-1097(03)00344-6 Fems Microbiol Lett 223:53-60 (2003)
PubMed id: 12799000  
 
 
Tetratricopeptide-like repeats in type-III-secretion chaperones and regulators.
M.J.Pallen, M.S.Francis, K.Fütterer.
 
  ABSTRACT  
 
Efficient type-III secretion depends on cytosolic molecular chaperones, which bind specifically to the translocators and effectors. In the past there has been a tendency to shoe-horn all type-III-secretion chaperones into a single structural and functional class. However, we have shown that the LcrH/SycD-like chaperones consist of three central tetratricopeptide-like repeats that are predicted to fold into an all-alpha-helical array that is quite distinct from the known structure of the SycE class of chaperones. Furthermore, we predict that this array creates a peptide-binding groove that is utterly different from the helix-binding groove in SycE. We present a homology model of LcrH/SycD that is consistent with existing mutagenesis data. We also report the existence of tetratricopeptide-like repeats in regulators of type-III secretion, such as HilA from Salmonella enterica and HrpB from Ralstonia solanacearum. The discovery of tetratricopeptide-like repeats in type-III-secretion regulators and chaperones provides a new conceptual framework for structural and mutagenesis studies and signals a potential unification of prokaryotic and eukaryotic chaperone biology.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19716705 A.M.Spear, N.J.Loman, H.S.Atkins, and M.J.Pallen (2009).
Microbial TIR domains: not necessarily agents of subversion?
  Trends Microbiol, 17, 393-398.  
19478065 M.Lunelli, R.K.Lokareddy, A.Zychlinsky, and M.Kolbe (2009).
IpaB-IpgC interaction defines binding motif for type III secretion translocator.
  Proc Natl Acad Sci U S A, 106, 9661-9666.
PDB codes: 3gyz 3gz1
19530229 Y.W.Tan, H.B.Yu, J.Sivaraman, K.Y.Leung, and Y.K.Mok (2009).
Mapping of the chaperone AcrH binding regions of translocators AopB and AopD and characterization of oligomeric and metastable AcrH-AopB-AopD complexes in the type III secretion system of Aeromonas hydrophila.
  Protein Sci, 18, 1724-1734.  
18165300 H.J.Betts, L.E.Twiggs, M.S.Sal, P.B.Wyrick, and K.A.Fields (2008).
Bioinformatic and biochemical evidence for the identification of the type III secretion system needle protein of Chlamydia trachomatis.
  J Bacteriol, 190, 1680-1690.  
18281060 P.Sun, J.E.Tropea, B.P.Austin, S.Cherry, and D.S.Waugh (2008).
Structural characterization of the Yersinia pestis type III secretion system needle protein YscF in complex with its heterodimeric chaperone YscE/YscG.
  J Mol Biol, 377, 819-830.
PDB code: 2p58
18923554 R.A.Daly, and C.P.Lostroh (2008).
Genetic analysis of the Salmonella transcription factor HilA.
  Can J Microbiol, 54, 854-860.  
17578515 E.Faudry, V.Job, A.Dessen, I.Attree, and V.Forge (2007).
Type III secretion system translocator has a molten globule conformation both in its free and chaperone-bound forms.
  FEBS J, 274, 3601-3610.  
16487320 J.E.Bröms, P.J.Edqvist, A.Forsberg, and M.S.Francis (2006).
Tetratricopeptide repeats are essential for PcrH chaperone function in Pseudomonas aeruginosa type III secretion.
  FEMS Microbiol Lett, 256, 57-66.  
16359316 P.J.Edqvist, J.E.Bröms, H.J.Betts, A.Forsberg, M.J.Pallen, and M.S.Francis (2006).
Tetratricopeptide repeats in the type III secretion chaperone, LcrH: their role in substrate binding and secretion.
  Mol Microbiol, 59, 31-44.  
15629918 A.Slepenkin, L.M.de la Maza, and E.M.Peterson (2005).
Interaction between components of the type III secretion system of Chlamydiaceae.
  J Bacteriol, 187, 473-479.  
16267298 J.E.Bröms, P.J.Edqvist, K.E.Carlsson, A.Forsberg, and M.S.Francis (2005).
Mapping of a YscY binding domain within the LcrH chaperone that is required for regulation of Yersinia type III secretion.
  J Bacteriol, 187, 7738-7752.  
16159780 K.A.Fields, E.R.Fischer, D.J.Mead, and T.Hackstadt (2005).
Analysis of putative Chlamydia trachomatis chaperones Scc2 and Scc3 and their use in the identification of type III secretion substrates.
  J Bacteriol, 187, 6466-6478.  
15757514 M.J.Pallen, S.A.Beatson, and C.M.Bailey (2005).
Bioinformatics analysis of the locus for enterocyte effacement provides novel insights into type-III secretion.
  BMC Microbiol, 5, 9.  
15808742 M.J.Pallen, S.A.Beatson, and C.M.Bailey (2005).
Bioinformatics, genomics and evolution of non-flagellar type-III secretion systems: a Darwinian perspective.
  FEMS Microbiol Rev, 29, 201-229.  
16000312 M.Locher, B.Lehnert, K.Krauss, J.Heesemann, M.Groll, and G.Wilharm (2005).
Crystal structure of the Yersinia enterocolitica type III secretion chaperone SycT.
  J Biol Chem, 280, 31149-31155.
PDB code: 2bho
15272862 A.P.Tampakaki, V.E.Fadouloglou, A.D.Gazi, N.J.Panopoulos, and M.Kokkinidis (2004).
Conserved features of type III secretion.
  Cell Microbiol, 6, 805-816.  
15150243 C.P.Ren, R.R.Chaudhuri, A.Fivian, C.M.Bailey, M.Antonio, W.M.Barnes, and M.J.Pallen (2004).
The ETT2 gene cluster, encoding a second type III secretion system from Escherichia coli, is present in the majority of strains but has undergone widespread mutational attrition.
  J Bacteriol, 186, 3547-3560.  
15488386 H.J.Betts, R.R.Chaudhuri, and M.J.Pallen (2004).
An analysis of type-III secretion gene clusters in Chromobacterium violaceum.
  Trends Microbiol, 12, 476-482.  
15271914 P.Bandyopadhyay, H.Xiao, H.A.Coleman, A.Price-Whelan, and H.M.Steinman (2004).
Icm/dot-independent entry of Legionella pneumophila into amoeba and macrophage hosts.
  Infect Immun, 72, 4541-4551.  
15590783 P.Ghosh (2004).
Process of protein transport by the type III secretion system.
  Microbiol Mol Biol Rev, 68, 771-795.  
14572546 M.J.Pallen, R.R.Chaudhuri, and I.R.Henderson (2003).
Genomic analysis of secretion systems.
  Curr Opin Microbiol, 6, 519-527.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.

 

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