PDBsum entry 2nsc

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protein links
Chaperone PDB id
Protein chain
109 a.a. *
Waters ×138
* Residue conservation analysis
PDB id:
Name: Chaperone
Title: Structures of and interactions between domains of trigger fa themotoga maritima
Structure: Trigger factor. Chain: a. Synonym: tf. Engineered: yes
Source: Thermotoga maritima. Organism_taxid: 2336. Gene: tig. Expressed in: escherichia coli. Expression_system_taxid: 562.
2.20Å     R-factor:   0.195     R-free:   0.260
Authors: E.Martinez-Hackert,W.A.Hendrickson
Key ref:
E.Martinez-Hackert and W.A.Hendrickson (2007). Structures of and interactions between domains of trigger factor from Thermotoga maritima. Acta Crystallogr D Biol Crystallogr, 63, 536-547. PubMed id: 17372359 DOI: 10.1107/S090744490700964X
03-Nov-06     Release date:   27-Mar-07    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
Q9WZF8  (TIG_THEMA) -  Trigger factor
425 a.a.
109 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Peptidylprolyl isomerase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Peptidylproline (omega=180) = peptidylproline (omega=0)
Peptidylproline (omega=180)
= peptidylproline (omega=0)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     protein transport   2 terms 


    Added reference    
DOI no: 10.1107/S090744490700964X Acta Crystallogr D Biol Crystallogr 63:536-547 (2007)
PubMed id: 17372359  
Structures of and interactions between domains of trigger factor from Thermotoga maritima.
E.Martinez-Hackert, W.A.Hendrickson.
Trigger factor (TF) is a eubacterial chaperone that associates with ribosomes at the peptide-exit tunnel and also occurs in excess free in the cytosol. TF is a three-domain protein that appears to exist in a dynamic equilibrium of oligomerization states and interdomain conformations. X-ray crystallography and chemical cross-linking were used to study the roles of the N- and C-terminal domains of Thermotoga maritima TF in TF oligomerization and chaperone activity. The structural conservation of both the N- and C-terminal TF domains was unambiguously established. The biochemical and crystallographic data reveal a tendency for these domains to partake in diverse and apparently nonspecific protein-protein interactions. It is found that the T. maritima and Escherichia coli TF surfaces lack evident exposed hydrophobic patches. Taken together, these data suggest that TF chaperones could interact with nascent proteins via hydrophilic surfaces.
  Selected figure(s)  
Figure 3.
Figure 3 Structural analysis of the N-terminal domain of T. maritima TF (tmTF[N]). (a) Ribbon diagram of a tmTF[N] protomer based on the 2.2 Å resolution crystal structure. The domain has an elongated + structure, which includes a four-stranded antiparallel -sheet (red) on one face of the molecule, two large -helices (blue) on the opposing face and nonregular segments (yellow). The cyan arrow marks the ribosome-binding loop. This model was built by replacing the C-terminal -strand with that of a symmetry-related tmTF[N]. We refer to this pseudo-protomer in our discussions of monomeric tmTF[N]. (b) The C-terminal -strand (red) from one tmTF[N] chain is swapped with the corresponding -strand of a symmetry-related molecule (grey). (c) Stereo diagram showing a superposition of C^ -backbone traces of four TF N-terminal domain structures: tmTF[N] (red), ecTF[N] (blue), vcTF[N] (green) and drTF[N] (yellow). The orientations of the first TF -helix and the ribosome-binding loop account for the most pronounced differences among the four TF[N] structures. (d) Ribbon diagram of E. coli Hsp33 oriented to have portions in common with tmTF[N] (strands, red; helices, blue; nonregular segments, yellow) placed as in (a). Elements not included in tmTF[N] are colored grey. The tmTF[N] and E. coli Hsp33 structures are surprisingly similar, with an r.m.s.d. of 2.8 Å. (e) Ribbon diagram of the tmTF[C] structure oriented with one of its helical protrusions (blue) placed as in the helical portion of tmTF[N] in (a). The tmTF[N] -helical structure superimposes very well with the helical protrusions that form the core of the tmTF[C] structure.
Figure 6.
Figure 6 Electrostatic surface potential of the TF N- and C-terminal domains calculated with the program GRASP. (a) TF N-terminal domains. A ribbon diagram of tmTF[N] is shown for reference (left) and electrostatic surface potentials are shown for tmTF[N] (middle) and for ecTF[N] (right). (b) Orthogonal view of (a). The ribosome-binding loop is marked by a cyan arrow and characterized by a positively charged surface (blue). The overall TF N-terminal domain structure appears positively charged (red), with few exposed hydrophobic surfaces or patches (light grey). (c) TF C-terminal domains. A ribbon diagram of tmTF[C] is shown for reference (left) and electrostatic surface potentials are shown for tmTF[C] (middle) and for ecTF[C] (right). This view highlights the concave surface in the C-terminal domain. The mostly negatively charged surface (red) is interspersed with small positive (blue) and hydrophobic (light grey) patches. Some positive patches, identified by green arrows, appear to be conserved.
  The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2007, 63, 536-547) copyright 2007.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19737520 E.Martinez-Hackert, and W.A.Hendrickson (2009).
Promiscuous substrate recognition in folding and assembly activities of the trigger factor chaperone.
  Cell, 138, 923-934.
PDB codes: 3gty 3gu0
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