PDBsum entry 2b1l

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Oxidoreductase PDB id
Protein chains
128 a.a. *
Waters ×139
* Residue conservation analysis
PDB id:
Name: Oxidoreductase
Title: Crystal structure of n-terminal 57 residue deletion mutant of e. Coli ccmg protein(residues 58-185)
Structure: Thiol:disulfide interchange protein dsbe. Chain: a, b. Synonym: ccmg protein, cytochromE C biogenesis protein ccmg. Engineered: yes. Mutation: yes. Other_details: n-terminal 57 residue deletion mutant
Source: Escherichia coli. Organism_taxid: 562. Gene: ccmg. Expressed in: escherichia coli. Expression_system_taxid: 562.
1.90Å     R-factor:   0.193     R-free:   0.231
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
16-Sep-05     Release date:   05-Sep-06    
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Protein chains
Pfam   ArchSchema ?
P0AA86  (DSBE_ECOLI) -  Thiol:disulfide interchange protein DsbE
185 a.a.
128 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     outer membrane-bounded periplasmic space   1 term 
  Biological process     cell redox homeostasis   2 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.
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.  
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