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Electron transport PDB id
1i5g
Jmol
Contents
Protein chain
144 a.a. *
Ligands
TRS
TS5
Waters ×279
* Residue conservation analysis
PDB id:
1i5g
Name: Electron transport
Title: Tryparedoxin ii complexed with glutathionylspermidine
Structure: Tryparedoxin ii. Chain: a. Engineered: yes. Mutation: yes
Source: Crithidia fasciculata. Organism_taxid: 5656. Strain: hs6. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.40Å     R-factor:   0.170     R-free:   0.203
Authors: B.Hofmann,H.Budde,K.Bruns,S.A.Guerrero,H.M.Kalisz,U.Menge, M.Montemartini,E.Nogoceke,P.Steinert,J.B.Wissing,L.Flohe,H. J.Hecht
Key ref: B.Hofmann et al. (2001). Structures of tryparedoxins revealing interaction with trypanothione. Biol Chem, 382, 459-471. PubMed id: 11347894 DOI: 10.1515/BC.2001.056
Date:
27-Feb-01     Release date:   14-Mar-01    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
O77093  (O77093_CRIFA) -  Tryparedoxin II
Seq:
Struc: 		165 a.a.
144 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     oxidation-reduction process   1 term 
  Biochemical function     antioxidant activity     2 terms  

 

 
DOI no: 10.1515/BC.2001.056 Biol Chem 382:459-471 (2001)
PubMed id: 11347894  
 
 
Structures of tryparedoxins revealing interaction with trypanothione.
B.Hofmann, H.Budde, K.Bruns, S.A.Guerrero, H.M.Kalisz, U.Menge, M.Montemartini, E.Nogoceke, P.Steinert, J.B.Wissing, L.Flohé, H.J.Hecht.
 
  ABSTRACT  
 
Tryparedoxins (TXNs) catalyse the reduction of peroxiredoxin-type peroxidases by the bis-glutathionyl derivative of spermidine, trypanothione, and are relevant to hydroperoxide detoxification and virulence of trypanosomes. The 3D-structures of the following tryparedoxins are presented: authentic tryparedoxin1 of Crithidia fasciculata, CfTXN1; the his-tagged recombinant protein, CfTXN1H6; reduced and oxidised CfTXN2, and an alternative substrate derivative of the mutein CfTXN2H6-Cys44Ser. Cys41 (Cys40 in TXN1) of the active site motif 40-WCPPCR-45 proved to be the only solvent-exposed redox active residue in CfTXN2. In reduced TXNs, its nucleophilicity is increased by a network of hydrogen bonds. In oxidised TXNs it can be attacked by the thiol of the 1N-glutathionyl residue of trypanothione, as evidenced by the structure of 1N-glutathionylspermidine-derivatised CfTXN2H6-Cys44Ser. Modelling suggests Arg45 (44), Glu73 (72), the Ile110 (109) cis-Pro111 (110)-bond and Arg129 (128) to be involved in the binding of trypanothione to CfTXN2 (CfTXN1). The model of TXN-substrate interaction is consistent with functional characteristics of known and newly designed muteins (CfTXN2H6-Arg129Asp and Glu73Arg) and the 1N-glutathionyl-spermidine binding in the CfTXN2H6-Cys44Ser structure.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20932300 B.Rüping, A.M.Ernst, S.B.Jekat, S.Nordzieke, A.R.Reineke, B.Müller, E.Bornberg-Bauer, D.Prüfer, and G.A.Noll (2010).
Molecular and phylogenetic characterization of the sieve element occlusion gene family in Fabaceae and non-Fabaceae plants.
  BMC Plant Biol, 10, 219.  
20838623 H.Castro, S.Romao, S.Carvalho, F.Teixeira, C.Sousa, and A.M.Tomás (2010).
Mitochondrial redox metabolism in trypanosomatids is independent of tryparedoxin activity.
  PLoS One, 5, e12607.  
18684708 J.Melchers, M.Diechtierow, K.Fehér, I.Sinning, I.Tews, R.L.Krauth-Siegel, and C.Muhle-Goll (2008).
Structural Basis for a Distinct Catalytic Mechanism in Trypanosoma brucei Tryparedoxin Peroxidase.
  J Biol Chem, 283, 30401-30411.
PDB codes: 2rm5 2rm6 3dwv
17567240 Y.Funato, and H.Miki (2007).
Nucleoredoxin, a novel thioredoxin family member involved in cell growth and differentiation.
  Antioxid Redox Signal, 9, 1035-1057.  
  17012768 T.Jaeger, and L.Flohé (2006).
The thiol-based redox networks of pathogens: unexploited targets in the search for new drugs.
  Biofactors, 27, 109-120.  
15537651 M.Comini, U.Menge, J.Wissing, and L.Flohé (2005).
Trypanothione synthesis in crithidia revisited.
  J Biol Chem, 280, 6850-6860.  
15054099 C.Meunier-Jamin, U.Kapp, G.A.Leonard, and S.McSweeney (2004).
The structure of the organic hydroperoxide resistance protein from Deinococcus radiodurans. Do conformational changes facilitate recycling of the redox disulfide?
  J Biol Chem, 279, 25830-25837.
PDB code: 1usp
14674746 D.Krumme, H.Budde, H.J.Hecht, U.Menge, O.Ohlenschläger, A.Ross, J.Wissing, V.Wray, and L.Flohé (2003).
NMR studies of the interaction of tryparedoxin with redox-inactive substrate homologues.
  Biochemistry, 42, 14720-14728.
PDB code: 1okd
12751791 H.Budde, L.Flohé, H.J.Hecht, B.Hofmann, M.Stehr, J.Wissing, and H.Lünsdorf (2003).
Kinetics and redox-sensitive oligomerisation reveal negative subunit cooperativity in tryparedoxin peroxidase of Trypanosoma brucei brucei.
  Biol Chem, 384, 619-633.  
  12897431 H.Budde, and L.Flohé (2003).
Enzymes of the thiol-dependent hydroperoxide metabolism in pathogens as potential drug targets.
  Biofactors, 17, 83-92.  
12702727 J.König, K.Lotte, R.Plessow, A.Brockhinke, M.Baier, and K.J.Dietz (2003).
Reaction mechanism of plant 2-Cys peroxiredoxin. Role of the C terminus and the quaternary structure.
  J Biol Chem, 278, 24409-24420.  
  14757972 L.Flohé, H.Budde, and B.Hofmann (2003).
Peroxiredoxins in antioxidant defense and redox regulation.
  Biofactors, 19, 3.  
12707277 M.S.Alphey, M.Gabrielsen, E.Micossi, G.A.Leonard, S.M.McSweeney, R.B.Ravelli, E.Tetaud, A.H.Fairlamb, C.S.Bond, and W.N.Hunter (2003).
Tryparedoxins from Crithidia fasciculata and Trypanosoma brucei: photoreduction of the redox disulfide using synchrotron radiation and evidence for a conformational switch implicated in function.
  J Biol Chem, 278, 25919-25925.
PDB codes: 1o73 1o7u 1o85 1o8w 1o8x 1oc8 1oc9
12751784 R.L.Krauth-Siegel, S.K.Meiering, and H.Schmidt (2003).
The parasite-specific trypanothione metabolism of trypanosoma and leishmania.
  Biol Chem, 384, 539-549.  
12791697 S.R.Wilkinson, D.Horn, S.R.Prathalingam, and J.M.Kelly (2003).
RNA interference identifies two hydroperoxide metabolizing enzymes that are essential to the bloodstream form of the african trypanosome.
  J Biol Chem, 278, 31640-31646.  
11839187 A.H.Fairlamb (2002).
Metabolic pathway analysis in trypanosomes and malaria parasites.
  Philos Trans R Soc Lond B Biol Sci, 357, 101-107.  
12033427 B.Hofmann, H.J.Hecht, and L.Flohé (2002).
Peroxiredoxins.
  Biol Chem, 383, 347-364.  
11752776 E.Micossi, W.N.Hunter, and G.A.Leonard (2002).
De novo phasing of two crystal forms of tryparedoxin II using the anomalous scattering from S atoms: a combination of small signal and medium resolution reveals this to be a general tool for solving protein crystal structures.
  Acta Crystallogr D Biol Crystallogr, 58, 21-28.
PDB codes: 1o6j 1o81
  12446214 H.Castro, H.Budde, L.Flohé, B.Hofmann, H.Lünsdorf, J.Wissing, and A.M.Tomás (2002).
Specificity and kinetics of a mitochondrial peroxiredoxin of Leishmania infantum.
  Free Radic Biol Med, 33, 1563-1574.  
11867629 N.Reckenfelderbäumer, and R.L.Krauth-Siegel (2002).
Catalytic properties, thiol pK value, and redox potential of Trypanosoma brucei tryparedoxin.
  J Biol Chem, 277, 17548-17555.  
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.