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Oxidoreductase PDB id
2f9s
Jmol
Contents
Protein chains
138 a.a. *
Waters ×171
* Residue conservation analysis
PDB id:
2f9s
Name: Oxidoreductase
Title: 2nd crystal structure of a soluble domain of resa in the oxidised form
Structure: Thiol-disulfide oxidoreductase resa. Chain: a, b. Fragment: soluble extracellular domain. Engineered: yes
Source: Bacillus subtilis. Organism_taxid: 1423. Gene: resa. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.40Å     R-factor:   0.163     R-free:   0.175
Authors: C.L.Colbert,Q.Wu,P.J.A.Erbel,K.H.Gardner,J.Deisenhofer
Key ref:
C.L.Colbert et al. (2006). Mechanism of substrate specificity in Bacillus subtilis ResA, a thioredoxin-like protein involved in cytochrome c maturation. Proc Natl Acad Sci U S A, 103, 4410-4415. PubMed id: 16537372 DOI: 10.1073/pnas.0600552103
Date:
06-Dec-05     Release date:   18-Apr-06    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P35160  (RESA_BACSU) -  Thiol-disulfide oxidoreductase resA
Seq:
Struc: 		179 a.a.
138 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

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

 

 
DOI no: 10.1073/pnas.0600552103 Proc Natl Acad Sci U S A 103:4410-4415 (2006)
PubMed id: 16537372  
 
 
Mechanism of substrate specificity in Bacillus subtilis ResA, a thioredoxin-like protein involved in cytochrome c maturation.
C.L.Colbert, Q.Wu, P.J.Erbel, K.H.Gardner, J.Deisenhofer.
 
  ABSTRACT  
 
The covalent attachment of heme cofactors to the apo-polypeptides via thioether bonds is unique to the maturation of c-type cytochromes. A number of thiol-disulfide oxidoreductases prepare the apocytochrome for heme insertion in system I and II cytochrome c maturation. Although most thiol-disulfide oxidoreductases are nonspecific, the less common, specific thiol-disulfide oxidoreductases may be key to directing the usage of electrons. Here we demonstrate that unlike other thiol-disulfide oxidoreductases, the protein responsible for reducing oxidized apocytochrome c in Bacillus subtilis, ResA, is specific for cytochrome c550 and utilizes alternate conformations to recognize redox partners. We report solution NMR evidence that ResA undergoes a redox-dependent conformational change between oxidation states, as well as data showing that ResA utilizes a surface cavity present only in the reduced state to recognize a peptide derived from cytochrome c550. Finally, we confirm that ResA is a specific thiol-disulfide oxidoreductase by comparing its reactivity to our mimetic peptide with its reactivity to oxidized glutathione, a nonspecific substrate. This study biochemically demonstrates the specificity of this thiol-disulfide oxidoreductase and enables us to outline a structural mechanism of regulating the usage of electrons in a thiol-disulfide oxidoreductase system.
 
  Selected figure(s)  
 
Figure 2.
Fig. 2. Residues affected by the redox state of htsResA. (a) Chemical shift changes of the assigned 1H/15N values for the backbone amide groups are plotted versus residue number. The color-coded bar denotes shift changes of 0.21 ppm (blue), 0.21-0.42 ppm (cyan), 0.42-0.63 ppm (lime-green), 0.63-0.84 ppm (green), 0.84-1.05 ppm (yellow), and 1.05 ppm (red) with the colored lines corresponding to the lower boundaries of each range. (b) The ribbon diagrams of htsResA[ox] are color-coded by 1H/15N chemical shift changes according to the color-coded bar in a. Black denotes locations of unassigned or proline residues. (c) Chemical shift changes between htsResA[red] and htsResA[ox] of the assigned 13C values for C and C carbons are plotted versus residue number. The color-coded bar denotes shift changes of 0.51 ppm (blue), 0.51-1.02 ppm (cyan), 1.02-1.53 ppm (green), 1.53-2.04 ppm (yellow), and 2.04 ppm (red) with the colored lines corresponding to the lower boundaries of each range. (d) The ribbon diagrams of htsResA[ox] are color-coded by 13C chemical shift changes according to the color-coded bar in c. Black denotes unassigned residues. 		Figure 4.
Fig. 4. Determination of the midpoint potential of the mimetic peptide at pH 6.9. The solid line represents a fit to the Nernst equation, n = 2. This gave an E[m] value of -332 mV.
 
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20382024 C.Sanders, S.Turkarslan, D.W.Lee, and F.Daldal (2010).
Cytochrome c biogenesis: the Ccm system.
  Trends Microbiol, 18, 266-274.  
20214494 G.Bonnard, V.Corvest, E.H.Meyer, and P.P.Hamel (2010).
Redox processes controlling the biogenesis of c-type cytochromes.
  Antioxid Redox Signal, 13, 1385-1401.  
19389711 J.J.Paxman, N.A.Borg, J.Horne, P.E.Thompson, Y.Chin, P.Sharma, J.S.Simpson, J.Wielens, S.Piek, C.M.Kahler, H.Sakellaris, M.Pearce, S.P.Bottomley, J.Rossjohn, and M.J.Scanlon (2009).
The structure of the bacterial oxidoreductase enzyme DsbA in complex with a peptide reveals a basis for substrate specificity in the catalytic cycle of DsbA enzymes.
  J Biol Chem, 284, 17835-17845.
PDB code: 3dks
19237745 Y.Carius, D.Rother, C.G.Friedrich, and A.J.Scheidig (2009).
The structure of the periplasmic thiol-disulfide oxidoreductase SoxS from Paracoccus pantotrophus indicates a triple Trx/Grx/DsbC functionality in chemotrophic sulfur oxidation.
  Acta Crystallogr D Biol Crystallogr, 65, 229-240.  
18377657 A.V.Lobanov, D.L.Hatfield, and V.N.Gladyshev (2008).
Reduced reliance on the trace element selenium during evolution of mammals.
  Genome Biol, 9, R62.  
18786143 S.Turkarslan, C.Sanders, S.Ekici, and F.Daldal (2008).
Compensatory thio-redox interactions between DsbA, CcdA and CcmG unveil the apocytochrome c holdase role of CcmG during cytochrome c maturation.
  Mol Microbiol, 70, 652-666.  
17122341 C.Sanders, C.Boulay, and F.Daldal (2007).
Membrane-spanning and periplasmic segments of CcmI have distinct functions during cytochrome c Biogenesis in Rhodobacter capsulatus.
  J Bacteriol, 189, 789-800.  
17189364 H.Geng, Y.Zhu, K.Mullen, C.S.Zuber, and M.M.Nakano (2007).
Characterization of ResDE-dependent fnr transcription in Bacillus subtilis.
  J Bacteriol, 189, 1745-1755.  
17177418 N.Metanis, E.Keinan, and P.E.Dawson (2006).
Synthetic seleno-glutaredoxin 3 analogues are highly reducing oxidoreductases with enhanced catalytic efficiency.
  J Am Chem Soc, 128, 16684-16691.  
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.