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PDBsum entry 2hzf

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protein Protein-protein interface(s) links
Electron transport, oxidoreductase PDB id
2hzf
Jmol
Contents
Protein chains
110 a.a. *
Waters ×148
* Residue conservation analysis
PDB id:
2hzf
Name: Electron transport, oxidoreductase
Title: Crystal structures of a poxviral glutaredoxin in the oxidize reduced states show redox-correlated structural changes
Structure: Glutaredoxin-1. Chain: a, b. Engineered: yes
Source: Ectromelia virus. Organism_taxid: 265874. Strain: moscow. Gene: evm053. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.80Å     R-factor:   0.182     R-free:   0.219
Authors: J.P.Bacik,B.Hazes
Key ref:
J.P.Bacik and B.Hazes (2007). Crystal structures of a poxviral glutaredoxin in the oxidized and reduced states show redox-correlated structural changes. J Mol Biol, 365, 1545-1558. PubMed id: 17137595 DOI: 10.1016/j.jmb.2006.11.002
Date:
08-Aug-06     Release date:   21-Nov-06    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q8JLF5  (GLRX1_ECTVM) -  Glutaredoxin-1
Seq:
Struc:
108 a.a.
110 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     virion   1 term 
  Biological process     oxidation-reduction process   2 terms 
  Biochemical function     electron carrier activity     2 terms  

 

 
DOI no: 10.1016/j.jmb.2006.11.002 J Mol Biol 365:1545-1558 (2007)
PubMed id: 17137595  
 
 
Crystal structures of a poxviral glutaredoxin in the oxidized and reduced states show redox-correlated structural changes.
J.P.Bacik, B.Hazes.
 
  ABSTRACT  
 
Glutaredoxins act as reducing agents for the large subunit of ribonucleotide reductase (R1) in many prokaryotes and eukaryotes, including humans. The same relationship has been proposed for the glutaredoxin and R1 proteins expressed by all orthopoxviruses, including vaccinia, variola, and ectromelia virus. Interestingly, the orthopoxviral proteins share 45% and 78% sequence identity with human glutaredoxin-1 (Grx-1) and R1, respectively. To study structure-function relationships of the vertebrate Grx-1 family, and reveal potential viral adaptations, we have determined crystal structures of the ectromelia virus glutaredoxin, EVM053, in the oxidized and reduced states. The structures show a large redox-induced conformational rearrangement of Tyr21 and Thr22 near the active site. We predict that the movement of Tyr21 is a viral-specific adaptation that increases the redox potential by stabilizing the reduced state. The conformational switch of Thr22 appears to be shared by vertebrate Grx-1 and may affect the strictly conserved Lys20. A crystal packing-induced structural change in residues 68-70 affects the GSH-binding loop, and our structures reveal a potential interaction network that connects the GSH-binding loop and the active site. EVM053 also exhibits a novel cis-proline (Pro53) in a loop that has been shown to contribute to R1-binding in Escherichia coli Grx-1. The cis-peptide bond of Pro53 may be required to promote electrostatic interactions between Lys52 and the C-terminal carboxylate of R1. Finally, dimethylarsenite was covalently attached to Cys23 in one reduced EVM053 structure and our preliminary data show that EVM053 has dimethylarsenate reductase activity.
 
  Selected figure(s)  
 
Figure 1.
Figure 1. Cartoon representation of EVM053 in the oxidized conformation. Helices are shown as coils and strands as arrows. The disulfide bond formed by the active site cysteine residues is shown in orange and the cis-Pro53 is drawn in ball-and-stick format. This Figure was generated using MOLSCRIPT^67 and Raster3D.^68
Figure 2.
Figure 2. Electron density (2|F[obs]|–|F[calc]|) for the active site of EVM053 in the (a) oxidized; (b) reduced; (c) dimethylarsenylated states. The disulfide bond in the oxidized structure and the proposed hydrogen bond in the reduced structure are indicated by broken lines. This Figure was generated using Xfit^65 and Raster3D.^68
 
  The above figures are reprinted by permission from Elsevier: J Mol Biol (2007, 365, 1545-1558) copyright 2007.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20516625 L.Li, N.Cheng, K.D.Hirschi, and X.Wang (2010).
Structure of Arabidopsis chloroplastic monothiol glutaredoxin AtGRXcp.
  Acta Crystallogr D Biol Crystallogr, 66, 725-732.
PDB code: 3ipz
19706593 D.A.Gell, L.Feng, S.Zhou, P.D.Jeffrey, K.Bendak, A.Gow, M.J.Weiss, Y.Shi, and J.P.Mackay (2009).
A cis-proline in alpha-hemoglobin stabilizing protein directs the structural reorganization of alpha-hemoglobin.
  J Biol Chem, 284, 29462-29469.
PDB code: 3ia3
19946139 K.Van Vliet, M.R.Mohamed, L.Zhang, N.Y.Villa, S.J.Werden, J.Liu, and G.McFadden (2009).
Poxvirus proteomics and virus-host protein interactions.
  Microbiol Mol Biol Rev, 73, 730-749.  
18473363 J.Yu, N.N.Zhang, P.D.Yin, P.X.Cui, and C.Z.Zhou (2008).
Glutathionylation-triggered conformational changes of glutaredoxin Grx1 from the yeast Saccharomyces cerevisiae.
  Proteins, 72, 1077-1083.
PDB codes: 3c1r 3c1s
18186468 W.Mi, Y.H.Liang, L.Li, and X.D.Su (2008).
The crystal structure of human chloride intracellular channel protein 2: a disulfide bond with functional implications.
  Proteins, 71, 509-513.
PDB code: 2per
  17401194 J.Sheng, J.Ye, and B.P.Rosen (2007).
Crystallization and preliminary X-ray crystallographic analysis of Escherichia coliglutaredoxin 2 in complex with glutathione and of a cysteine-less variant without glutathione.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 63, 280-282.  
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