spacer
spacer

PDBsum entry 2g0f

Go to PDB code: 
protein links
Oxidoreductase PDB id
2g0f
Jmol
Contents
Protein chain
149 a.a. *
Waters ×58
* Residue conservation analysis
PDB id:
2g0f
Name: Oxidoreductase
Title: Crystal structure of p144a mutant of e.Coli ccmg protein
Structure: Thiol:disulfide interchange protein dsbe. Chain: a. Fragment: residues 36-184. Synonym: ccmg protein, cytochromE C biogenesis protein ccmg. Engineered: yes. Mutation: yes
Source: Escherichia coli. Organism_taxid: 562. Gene: ccmg. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.20Å     R-factor:   0.186     R-free:   0.238
Authors: N.Ouyang,Y.G.Gao,H.Y.Hu,Z.X.Xia
Key ref:
N.Ouyang et al. (2006). Crystal structures of E. coli CcmG and its mutants reveal key roles of the N-terminal beta-sheet and the fingerprint region. Proteins, 65, 1021-1031. PubMed id: 17019698 DOI: 10.1002/prot.21184
Date:
12-Feb-06     Release date:   05-Dec-06    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P0AA86  (DSBE_ECOLI) -  Thiol:disulfide interchange protein DsbE
Seq:
Struc:
185 a.a.
149 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!
  Cellular component     membrane   4 terms 
  Biological process     oxidation-reduction process   3 terms 
  Biochemical function     oxidoreductase activity     2 terms  

 

 
DOI no: 10.1002/prot.21184 Proteins 65:1021-1031 (2006)
PubMed id: 17019698  
 
 
Crystal structures of E. coli CcmG and its mutants reveal key roles of the N-terminal beta-sheet and the fingerprint region.
N.Ouyang, Y.G.Gao, H.Y.Hu, Z.X.Xia.
 
  ABSTRACT  
 
CcmG, also designated DsbE, functions as a periplasmic protein thiol:disulfide oxidoreductase and is required for cytochrome c maturation. Here we report the crystal structures of Escherichia coli CcmG and its two mutants, P144A and the N-terminal fifty seven-residue deletion mutant, and two additional deletion mutants were studied by circular dichroism. Structural comparison of E. coli CcmG with its deletion mutants reveals that the N-terminal beta-sheet is essential for maintaining the folding topology and consequently maintaining the active-site structure of CcmG. Pro144 and Glu145 are key residues of the fingerprint region of CcmG. Pro144 is in cis-configuration, and it makes van der Waals interactions with the active-site disulfide Cys80-Cys83 and forms a C--H...O hydrogen bond with Thr82, helping stabilize the active-site structure. Glu145 forms a salt-bridge and hydrogen-bond network with other residues of the fingerprint region and with Arg158, further stabilizing the active-site structure. The cis-configuration of Pro144 makes the backbone nitrogen and oxygen of Ala143 exposed to solvent, favorable for interacting with binding partners. The key role of cis-Pro144 is verified by the P144A mutant, which contains trans-Ala144 and displays redox property changes. Structural comparison of E. coli CcmG with the recently reported structure of CcmG in complex with the N-terminal domain of DsbD reveals that Tyr141 undergoes conformational changes upon binding DsbD. A cis-proline located at the N-terminus of the first beta-strand of the betabetaalpha motif of the thioredoxin-like domain is a conserved structural feature of the thioredoxin superfamily.
 
  Selected figure(s)  
 
Figure 5.
Figure 5. The active-site disulfide and the cis-proline loop of CcmG-EC in comparison with those of the P144A mutant and of DsbC in the DsbC-nDsbD complex. CcmG-EC is shown in red in the left panel, P144A in green in the central panel, DsbC in pink in the right pannel (the side-chain of Y100 in green for clarity), and nDsbD in blue in the three panels. The C H O hydrogen bond and interprotein hydrogen bonds are shown as dotted lines. This diagram was prepared using the program SETOR.
Figure 6.
Figure 6. Redox equilibrium of CcmG-EC (squares) and the P144A mutant (circles) with glutathione.
 
  The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2006, 65, 1021-1031) copyright 2006.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20544959 A.Di Matteo, N.Calosci, S.Gianni, P.Jemth, M.Brunori, and C.Travaglini-Allocatelli (2010).
Structural and functional characterization of CcmG from Pseudomonas aeruginosa, a key component of the bacterial cytochrome c maturation apparatus.
  Proteins, 78, 2213-2221.
PDB codes: 3kh7 3kh9
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.  
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
17933514 B.Heras, M.Kurz, S.R.Shouldice, and J.L.Martin (2007).
The name's bond......disulfide bond.
  Curr Opin Struct Biol, 17, 691-698.  
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.