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PDBsum entry 1hxv

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protein links
Chaperone PDB id
1hxv
Jmol PyMol
Contents
Protein chain
85 a.a. *
* Residue conservation analysis
PDB id:
1hxv
Name: Chaperone
Title: Ppiase domain of the mycoplasma genitalium trigger factor
Structure: Trigger factor. Chain: a. Fragment: ppiase domain (residues 150-250). Engineered: yes
Source: Mycoplasma genitalium. Organism_taxid: 2097. Expressed in: escherichia coli. Expression_system_taxid: 562.
NMR struc: 12 models
Authors: M.Vogtherr,T.N.Parac,M.Maurer,A.Pahl,K.Fiebig
Key ref:
M.Vogtherr et al. (2002). NMR solution structure and dynamics of the peptidyl-prolyl cis-trans isomerase domain of the trigger factor from Mycoplasma genitalium compared to FK506-binding protein. J Mol Biol, 318, 1097-1115. PubMed id: 12054805 DOI: 10.1016/S0022-2836(02)00112-2
Date:
17-Jan-01     Release date:   29-May-02    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P47480  (TIG_MYCGE) -  Trigger factor
Seq:
Struc:
444 a.a.
85 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.5.2.1.8  - 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   1 term 

 

 
    Added reference    
 
 
DOI no: 10.1016/S0022-2836(02)00112-2 J Mol Biol 318:1097-1115 (2002)
PubMed id: 12054805  
 
 
NMR solution structure and dynamics of the peptidyl-prolyl cis-trans isomerase domain of the trigger factor from Mycoplasma genitalium compared to FK506-binding protein.
M.Vogtherr, D.M.Jacobs, T.N.Parac, M.Maurer, A.Pahl, K.Saxena, H.Rüterjans, C.Griesinger, K.M.Fiebig.
 
  ABSTRACT  
 
We have solved the solution structure of the peptidyl-prolyl cis-trans isomerase (PPIase) domain of the trigger factor from Mycoplasma genitalium by homo- and heteronuclear NMR spectroscopy. Our results lead to a well-defined structure with a backbone rmsd of 0.23 A. As predicted, the PPIase domain of the trigger factor adopts the FK506 binding protein (FKBP) fold. Furthermore, our NMR relaxation data indicate that the dynamic behavior of the trigger factor PPIase domain and of FKBP are similar. Structural variations when compared to FKBP exist in the flap region and within the bulges of strand 5 of the beta sheet. Although the active-site crevice is similar to that of FKBP, subtle steric variations in this region can explain why FK506 does not bind to the trigger factor. Sequence variability (27% identity) between trigger factor and FKBP results in significant differences in surface charge distribution and the absence of the first strand of the central beta sheet. Our data indicate, however, that this strand may be partially structured as "nascent" beta strand. This makes the trigger factor PPIase domain the most minimal representative of the FKBP like protein family of PPIases.
 
  Selected figure(s)  
 
Figure 8.
Figure 8. Superposition of the lowest-energy solution structure of TF[PPIase] (blue) and the X-ray structure of FKBP (red). For FKBP the N terminus (residues 1-15) is omitted for clarity. Coordinates for FKBP were taken from the FKBP-FK506 complex, PDB entry 1FKF. The structures were superimposed using residues marked by asterisks in Figure 6, resulting in an rmsd value of 1.3 Å.
Figure 10.
Figure 10. Model of the hypothetical TF[PPIase]-FK506 complex (left) and comparison with the actual FKBP-FK506 complex (right). The hypothetical TF[PPIase]-FK506 complex is based upon the same superposition of TF[PPIase] and FKBP as in Figure 8. Regions of FK506 and of TF[PPIase] experiencing steric clashes are indicated by their dotted van der Waals surfaces. Blue, residues Phe66 and Tyr93 (TF[PPIase]) that interfere with the binding in TF[PPIase] and the corresponding Val55 and Tyr82 of FKBP. Regions of FK506 in conflict with the binding to TF[PPIase] are displayed in red and green, respectively, and are colored according to Scheme 1.
 
  The above figures are reprinted by permission from Elsevier: J Mol Biol (2002, 318, 1097-1115) copyright 2002.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19645725 L.Martino, Y.He, K.L.Hands-Taylor, E.R.Valentine, G.Kelly, C.Giancola, and M.R.Conte (2009).
The interaction of the Escherichia coli protein SlyD with nickel ions illuminates the mechanism of regulation of its peptidyl-prolyl isomerase activity.
  FEBS J, 276, 4529-4544.
PDB code: 2kfw
18065652 J.Stie, and D.Fox (2008).
Calcineurin regulation in fungi and beyond.
  Eukaryot Cell, 7, 177-186.  
18760284 V.Lamour, S.T.Rutherford, K.Kuznedelov, U.A.Ramagopal, R.L.Gourse, K.Severinov, and S.A.Darst (2008).
Crystal structure of Escherichia coli Rnk, a new RNA polymerase-interacting protein.
  J Mol Biol, 383, 367-379.
PDB code: 3bmb
18043871 Y.Yao, G.Bhabha, G.Kroon, M.Landes, and H.J.Dyson (2008).
Structure discrimination for the C-terminal domain of Escherichia coli trigger factor in solution.
  J Biomol NMR, 40, 23-30.  
17603821 B.Cutting, S.V.Shelke, Z.Dragic, B.Wagner, H.Gathje, S.Kelm, and B.Ernst (2007).
Sensitivity enhancement in saturation transfer difference (STD) experiments through optimized excitation schemes.
  Magn Reson Chem, 45, 720-724.  
17372359 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.
PDB codes: 2nsa 2nsb 2nsc
16585746 O.Musatovova, S.Dhandayuthapani, and J.B.Baseman (2006).
Transcriptional heat shock response in the smallest known self-replicating cell, Mycoplasma genitalium.
  J Bacteriol, 188, 2845-2855.  
15798974 A.Leonov, B.Voigt, F.Rodriguez-Castañeda, P.Sakhaii, and C.Griesinger (2005).
Convenient synthesis of multifunctional EDTA-based chiral metal chelates substituted with an S-mesylcysteine.
  Chemistry, 11, 3342-3348.  
15353602 A.V.Ludlam, B.A.Moore, and Z.Xu (2004).
The crystal structure of ribosomal chaperone trigger factor from Vibrio cholerae.
  Proc Natl Acad Sci U S A, 101, 13436-13441.
PDB code: 1t11
15334087 L.Ferbitz, T.Maier, H.Patzelt, B.Bukau, E.Deuerling, and N.Ban (2004).
Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins.
  Nature, 431, 590-596.
PDB codes: 1w26 1w2b
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 code is shown on the right.

 

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