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PDBsum entry 2fd2

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Electron transfer(iron-sulfur protein) PDB id
2fd2

 

 

 

 

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Contents
Protein chain
106 a.a. *
Ligands
SF4
F3S
Waters ×30
* Residue conservation analysis
PDB id:
2fd2
Name: Electron transfer(iron-sulfur protein)
Title: Crystallographic analysis of two site-directed mutants of azotobacter vinelandii ferredoxin
Structure: Ferredoxin. Chain: a. Engineered: yes
Source: Azotobacter vinelandii. Organism_taxid: 354
Resolution:
1.90Å     R-factor:   0.232    
Authors: C.D.Stout
Key ref: J.Soman et al. (1991). Crystallographic analysis of two site-directed mutants of Azotobacter vinelandii ferredoxin. J Biol Chem, 266, 21558-21562. PubMed id: 1939185
Date:
20-Aug-90     Release date:   15-Oct-90    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P00214  (FER1_AZOVI) -  Ferredoxin-1 from Azotobacter vinelandii
Seq:
Struc:
107 a.a.
106 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 

 
J Biol Chem 266:21558-21562 (1991)
PubMed id: 1939185  
 
 
Crystallographic analysis of two site-directed mutants of Azotobacter vinelandii ferredoxin.
J.Soman, S.Iismaa, C.D.Stout.
 
  ABSTRACT  
 
The crystal structure of the C24A mutant of Azotobacter vinelandii 7Fe ferredoxin (FdI) has been solved and refined at 2.0-A resolution. The structure is isomorphous to native FdI except at the site of mutation where A24 moves toward the [4Fe-4S] cluster. In spite of this inefficient packing results: three of five van der Waals contacts from the S gamma of C24 in native FdI are lost and the remaining two become longer. Consequently, the [4Fe-4S] cluster is either disordered or has a higher temperature factor (B factor) compared to the rest of the C24A FdI molecule. In addition, the entire C24A FdI structure has a higher overall B factor than native FdI. Therefore, in comparison to native FdI, the C24A mutant is isomorphous but exhibits large differences in B factor, especially at the [4Fe-4S] cluster. In contrast, the C20A FdI structure (Martin, A. G., Burgess, B. K., Stout, C. D., Cash, V. L., Dean, D. R., Jensen, G. M., and Stephens, P. J. (1990) Proc. Natl. Acad. Sci. U. S. A. 87, 598-602), which contains large structural rearrangements in the vicinity of the [4Fe-4S] cluster, exhibits essentially no change in B factor. The conformational change observed at residue 24 is similar in both C24A and C20A FdI structures. The solvent accessibility of the Fe atoms in the [3Fe-4S] and [4Fe-4S] clusters is similar in C24A, C20A, and native FdI.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19290553 E.Saridakis, P.Giastas, G.Efthymiou, V.Thoma, J.M.Moulis, P.Kyritsis, and I.M.Mavridis (2009).
Insight into the protein and solvent contributions to the reduction potentials of [4Fe-4S]2+/+ clusters: crystal structures of the Allochromatium vinosum ferredoxin variants C57A and V13G and the homologous Escherichia coli ferredoxin.
  J Biol Inorg Chem, 14, 783-799.
PDB codes: 2zvs 3eun 3exy
11463610 B.W.Beck, Q.Xie, and T.Ichiye (2001).
Sequence determination of reduction potentials by cysteinyl hydrogen bonds and peptide pipoles in [4Fe-4S] ferredoxins.
  Biophys J, 81, 601-613.  
1368439 J.A.Tainer, V.A.Roberts, and E.D.Getzoff (1992).
Protein metal-binding sites.
  Curr Opin Biotechnol, 3, 378-387.  
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.

 

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